Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T51282 | Target Info | |||
| Target Name | Rho-associated protein kinase 1 (ROCK1) | ||||
| Synonyms | Rok; Rho-associated, coiled-coil containing protein kinase 1; Rho-associated kinase 1; Rho kinase; ROCK1; ROCK; P160ROCK; P160(rock); P160 ROCK-1; Let-502 kinase | ||||
| Target Type | Successful Target | ||||
| Gene Name | ROCK1 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Ximelegatran | Ligand Info | |||||
| Structure Description | Crystal Structure of ROCK I bound to Y-27632 | PDB:2ETR | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEDK375 GEEETFPIPK385 AFVGNQLPFV395 GFTYYSNRRY405 |
|||||
|
|
||||||
| Ligand Name: H-1152 | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF ROCK I BOUND TO H-1152P A DI-METHYLATED VARIANT OF FASUDIL | PDB:3D9V | ||||
| Method | X-ray diffraction | Resolution | 3.30 Å | Mutation | No | [1] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEDK375 GEEETFPIPK385 AFVGNQLPFV395 GFTYYSNRRY405 |
|||||
|
|
||||||
| Ligand Name: Acid-activated omeprazole | Ligand Info | |||||
| Structure Description | Crystal Structure of ROCK 1 bound to hydroxyfasudil | PDB:2ETK | ||||
| Method | X-ray diffraction | Resolution | 2.96 Å | Mutation | No | [1] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEDK375 GEEETFPIPK385 AFVGNQLPFV395 GFTYYSNRRY405 |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HFS or .HFS2 or .HFS3 or :3HFS;style chemicals stick;color identity;select .A:82 or .A:90 or .A:103 or .A:105 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| Ligand Name: Fasudil | Ligand Info | |||||
| Structure Description | Crystal Structure of ROCK 1 bound to fasudil | PDB:2ESM | ||||
| Method | X-ray diffraction | Resolution | 3.20 Å | Mutation | No | [1] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEDK375 GEEETFPIPK385 AFVGNQLPFV395 GFTYYSNRRY405 |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .M77 or .M772 or .M773 or :3M77;style chemicals stick;color identity;select .A:82 or .A:83 or .A:90 or .A:103 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:160 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| Ligand Name: PMID28048944-Compound-19 | Ligand Info | |||||
| Structure Description | Human RHO-ASSOCIATED PROTEIN KINASE 1 (ROCK 1) IN COMPLEX WITH INDAZOLE DERIVATIVE (COMPOUND 18) | PDB:3V8S | ||||
| Method | X-ray diffraction | Resolution | 2.29 Å | Mutation | No | [2] |
| PDB Sequence |
ETRFEKMDNL
17 LRDPKSEVNS27 DCLLDGLDAL37 VYDLDFPALR47 KNKNIDNFLS57 RYKDTINKIR 67 DLRMKAEDYE77 VVKVIGRGAF87 GEVQLVRHKS97 TRKVYAMKLL107 SKFEMIKRSD 117 SAFFWEERDI127 MAFANSPWVV137 QLFYAFQDDR147 YLYMVMEYMP157 GGDLVNLMSN 167 YDVPEKWARF177 YTAEVVLALD187 AIHSMGFIHR197 DVKPDNMLLD207 KSGHLKLADF 217 GTCMKMNKEG227 MVRCDTAVGT237 PDYISPEVLK247 SQGGDGYYGR257 ECDWWSVGVF 267 LYEMLVGDTP277 FYADSLVGTY287 SKIMNHKNSL297 TFPDDNDISK307 EAKNLICAFL 317 TDREVRLGRN327 GVEEIKRHLF337 FKNDQWAWET347 LRDTVAPVVP357 DLSSDIDTSN 367 FDDLEEDKGE377 EETFPIPKAF387 VGNQLPFVGF397 TYYSN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .0HD or .0HD2 or .0HD3 or :30HD;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.753
GLY83
4.120
ARG84
3.750
GLY85
3.184
PHE87
4.802
GLY88
3.550
GLU89
3.606
VAL90
3.361
ALA103
3.384
LYS105
3.769
LEU106
4.605
|
|||||
| Ligand Name: RKI-1447 | Ligand Info | |||||
| Structure Description | Rho-associated protein kinase 1 (ROCK 1) IN COMPLEX WITH RKI1447 | PDB:3TWJ | ||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [3] |
| PDB Sequence |
FETRFEKMDN
16 LLRDPKSEVN26 SDCLLDGLDA36 LVYDLDFPAL46 RKNKNIDNFL56 SRYKDTINKI 66 RDLRMKAEDY76 EVVKVIGRGA86 FGEVQLVRHK96 STRKVYAMKL106 LSKFEMIKRS 116 DSAFFWEERD126 IMAFANSPWV136 VQLFYAFQDD146 RYLYMVMEYM156 PGGDLVNLMS 166 NYDVPEKWAR176 FYTAEVVLAL186 DAIHSMGFIH196 RDVKPDNMLL206 DKSGHLKLAD 216 FGTCMKMNKE226 GMVRCDTAVG236 TPDYISPEVL246 KSQGGDGYYG256 RECDWWSVGV 266 FLYEMLVGDT276 PFYADSLVGT286 YSKIMNHKNS296 LTFPDDNDIS306 KEAKNLICAF 316 LTDREVRLGR326 NGVEEIKRHL336 FFKNDQWAWE346 TLRDTVAPVV356 PDLSSDIDTS 366 NFDDLEEDKG376 EEETFPIPKA386 FVGNQLPFVG396 FTYYSN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .07R or .07R2 or .07R3 or :307R;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:124 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
4.984
GLY83
4.519
ARG84
3.781
GLY85
2.721
ALA86
4.153
PHE87
3.640
GLY88
2.770
GLU89
3.693
VAL90
3.227
ALA103
3.681
LYS105
2.886
LEU106
4.458
LEU107
3.848
|
|||||
| Ligand Name: AMP-PNP | Ligand Info | |||||
| Structure Description | Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure | PDB:2V55 | ||||
| Method | X-ray diffraction | Resolution | 3.71 Å | Mutation | No | [4] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEETF381 PIPKAFVGNQ391 LPFVGFTYYS401 NRR
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:90 or .A:103 or .A:105 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:160 or .A:198 or .A:200 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:237 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.747
GLY83
4.383
ARG84
4.803
GLY85
3.889
ALA86
3.011
PHE87
4.709
VAL90
4.141
ALA103
3.975
LYS105
3.158
VAL137
3.604
MET153
3.189
GLU154
3.318
|
|||||
| Ligand Name: N-[(2,3-dihydro-1,4-benzodioxin-5-yl)methyl]-4-(pyridin-4-yl)benzamide | Ligand Info | |||||
| Structure Description | Crystal structure of Rock1 with a pyridinylbenzamide based inhibitor | PDB:6E9W | ||||
| Method | X-ray diffraction | Resolution | 2.96 Å | Mutation | No | [5] |
| PDB Sequence |
TRFEKMDNLL
18 RDPKSEVNSD28 CLLDGLDALV38 YDLDFPALRK48 NKNIDNFLSR58 YKDTINKIRD 68 LRMKAEDYEV78 VKVIGRGAFG88 EVQLVRHKST98 RKVYAMKLLS108 KFEMIKRSDS 118 AFFWEERDIM128 AFANSPWVVQ138 LFYAFQDDRY148 LYMVMEYMPG158 GDLVNLMSNY 168 DVPEKWARFY178 TAEVVLALDA188 IHSMGFIHRD198 VKPDNMLLDK208 SGHLKLADFG 218 TCMKMNKEGM228 VRCDTAVGTP238 DYISPEVLKS248 YYGRECDWWS263 VGVFLYEMLV 273 GDTPFYADSL283 VGTYSKIMNH293 KNSLTFPDDN303 DISKEAKNLI313 CAFLTDREVR 323 LGRNGVEEIK333 RHLFFKNDQW343 AWETLRDTVA353 PVVPDLSSDI363 DTSNFDDLTF 381 PIPKAFVGNQ391 LPFVGFTYYS401 NRR
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J0P or .J0P2 or .J0P3 or :3J0P;style chemicals stick;color identity;select .A:82 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.466
ARG84
4.202
GLY85
3.646
ALA86
3.455
PHE87
3.252
GLY88
3.390
GLU89
3.611
VAL90
3.710
ALA103
3.760
LYS105
3.488
LEU106
4.049
LEU107
3.622
|
|||||
| Ligand Name: 1-(4-amino-1,2,5-oxadiazol-3-yl)-5-methyl-N-({3-[(5-methyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)carbamoyl]phenyl}methyl)-1H-1,2,3-triazole-4-carboxamide | Ligand Info | |||||
| Structure Description | X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR | PDB:5WNF | ||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [6] |
| PDB Sequence |
FETRFEKMDN
16 LLRDPKSEVN26 SDCLLDGLDA36 LVYDLDFPAL46 RKNKNIDNFL56 SRYKDTINKI 66 RDLRMKAEDY76 EVVKVIGRGA86 FGEVQLVRHK96 STRKVYAMKL106 LSKFEMIKRS 116 DSAFFWEERD126 IMAFANSPWV136 VQLFYAFQDD146 RYLYMVMEYM156 PGGDLVNLMS 166 NYDVPEKWAR176 FYTAEVVLAL186 DAIHSMGFIH196 RDVKPDNMLL206 DKSGHLKLAD 216 FGTCMKMNKE226 GMVRCDTAVG236 TPDYISPEVL246 KSQGGDGYYG256 RECDWWSVGV 266 FLYEMLVGDT276 PFYADSLVGT286 YSKIMNHKNS296 LTFPDDNDIS306 KEAKNLICAF 316 LTDREVRLGR326 NGVEEIKRHL336 FFKNDQWAWE346 TLRDTVAPVV356 PDLSSDIDTS 366 NFDDLEEDKG376 EEETFPIPKA386 FVGNQLPFVG396 FTYYS
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .B4V or .B4V2 or .B4V3 or :3B4V;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:117 or .A:120 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.518
GLY83
3.949
ARG84
3.876
GLY85
3.547
ALA86
3.511
PHE87
2.885
GLY88
3.638
GLU89
3.651
VAL90
3.463
ALA103
3.470
LYS105
3.887
LEU106
4.284
LEU107
3.529
|
|||||
| Ligand Name: 3,4-Dimethoxy-N-[3-(5-methyl-4,5,6,7-tetrahydro-thiazolo[5,4-c]pyridin-2-ylcarbamoyl)-benzyl]-benzamide | Ligand Info | |||||
| Structure Description | X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR | PDB:5WNE | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [7] |
| PDB Sequence |
MDNLLRDPKS
23 EVNSDCLLDG33 LDALVYDLDF43 PALRKNKNID53 NFLSRYKDTI63 NKIRDLRMKA 73 EDYEVVKVIG83 RGAFGEVQLV93 RHKSTRKVYA103 MKLLSKFEMI113 KRSDSAFFWE 123 ERDIMAFANS133 PWVVQLFYAF143 QDDRYLYMVM153 EYMPGGDLVN163 LMSNYDVPEK 173 WARFYTAEVV183 LALDAIHSMG193 FIHRDVKPDN203 MLLDKSGHLK213 LADFGTCMKM 223 NKEGMVRCDT233 AVGTPDYISP243 EVLKSQGGDG253 YYGRECDWWS263 VGVFLYEMLV 273 GDTPFYADSL283 VGTYSKIMNH293 KNSLTFPDDN303 DISKEAKNLI313 CAFLTDREVR 323 LGRNGVEEIK333 RHLFFKNDQW343 AWETLRDTVA353 PVVPDLSSDI363 DTSNFDDLEE 373 DEETFPIPKA386 FVGNQLPFVG396 FTYY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .B4J or .B4J2 or .B4J3 or :3B4J;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:117 or .A:120 or .A:124 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.589
GLY83
4.041
ARG84
4.206
GLY85
3.576
ALA86
3.388
PHE87
2.848
GLY88
3.810
GLU89
3.817
VAL90
3.508
ALA103
3.737
LYS105
3.003
LEU106
4.236
LEU107
3.641
ASP117
3.221
|
|||||
| Ligand Name: 2-[3-[3-(4-Methylpiperazin-1-Yl)propoxy]phenyl]-~{n}-[4-(1~{h}-Pyrrolo[2,3-B]pyridin-3-Yl)-1,3-Thiazol-2-Yl]ethanamide | Ligand Info | |||||
| Structure Description | ROCK 1 bound to azaindole thiazole piperazine inhibitor | PDB:5KKT | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [8] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKA 119 FFWEERDIMA129 FANSPWVVQL139 FYAFQDDRYL149 YMVMEYMPGG159 DLVNLMSNYD 169 VPEKWARFYT179 AEVVLALDAI189 HSMGFIHRDV199 KPDNMLLDKS209 GHLKLADFGT 219 CMKMNKEGMV229 RCDTAVGTPD239 YISPEVLKSQ249 GGDGYYGREC259 DWWSVGVFLY 269 EMLVGDTPFY279 ADSLVGTYSK289 IMNHKNSLTF299 PDDNDISKEA309 KNLICAFLTD 319 REVRLGRNGV329 EEIKRHLFFK339 NDQWAWETLR349 DTVAPVVPDL359 SSDIDTSNFD 369 DLETFPIPKA386 FVGNQLPFVG396 FTYYSNRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6U2 or .6U22 or .6U23 or :36U2;style chemicals stick;color identity;select .A:82 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:235 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.640
ARG84
4.011
GLY85
3.798
ALA86
3.808
PHE87
3.485
GLY88
3.488
GLU89
3.614
VAL90
3.450
ALA103
3.489
LYS105
2.961
LEU106
4.109
LEU107
3.659
PHE120
3.435
GLU124
4.200
|
|||||
| Ligand Name: 2-{3-[3-(Piperidin-4-Yl)propoxy]phenyl}-N-[4-(Pyridin-4-Yl)-1,3-Thiazol-2-Yl]acetamide | Ligand Info | |||||
| Structure Description | Rho-associated protein kinase 1 (ROCK 1) in complex with a pyridine thiazole piperidine inhibitor | PDB:5HVU | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [9] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEETF381 PIPKAFVGNQ391 LPFVGFTYYS401 NRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .65R or .65R2 or .65R3 or :365R;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:117 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:218 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.808
GLY83
4.581
ARG84
4.197
GLY85
3.699
PHE87
3.763
GLY88
3.259
GLU89
3.618
VAL90
3.610
ALA103
3.461
LYS105
2.834
LEU106
4.651
LEU107
3.650
ASP117
2.928
|
|||||
| Ligand Name: (2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide | Ligand Info | |||||
| Structure Description | X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR | PDB:5WNG | ||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [10] |
| PDB Sequence |
FETRFEKMDN
16 LLRDPKSEVN26 SDCLLDGLDA36 LVYDLDFPAL46 RKNKNIDNFL56 SRYKDTINKI 66 RDLRMKAEDY76 EVVKVIGRGA86 FGEVQLVRHK96 STRKVYAMKL106 LSKFEMIKRS 116 DSAFFWEERD126 IMAFANSPWV136 VQLFYAFQDD146 RYLYMVMEYM156 PGGDLVNLMS 166 NYDVPEKWAR176 FYTAEVVLAL186 DAIHSMGFIH196 RDVKPDNMLL206 DKSGHLKLAD 216 FGTCMKMNKE226 GMVRCDTAVG236 TPDYISPEVL246 KSQGGDGYYG256 RECDWWSVGV 266 FLYEMLVGDT276 PFYADSLVGT286 YSKIMNHKNS296 LTFPDDNDIS306 KEAKNLICAF 316 LTDREVRLGR326 NGVEEIKRHL336 FFKNDQWAWE346 TLRDTVAPVV356 PDLSSDIDTS 366 NFDDLEEDKG376 EEETFPIPKA386 FVGNQLPFVG396 FTYYS
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .B4Y or .B4Y2 or .B4Y3 or :3B4Y;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:117 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:202 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:235 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.545
GLY83
4.835
ARG84
3.720
GLY85
3.515
ALA86
3.567
PHE87
2.929
GLY88
3.750
GLU89
3.843
VAL90
3.413
ALA103
3.532
LYS105
3.454
LEU106
4.335
LEU107
3.480
ASP117
2.805
PHE120
3.447
|
|||||
| Ligand Name: N-[4-(2-Fluoropyridin-4-Yl)thiophen-2-Yl]-2-{3-[(Methylsulfonyl)amino]phenyl}acetamide | Ligand Info | |||||
| Structure Description | ROCK 1 bound to a pyridine thiazole inhibitor | PDB:5BML | ||||
| Method | X-ray diffraction | Resolution | 2.95 Å | Mutation | No | [11] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDISK307 EAKNLICAFL 317 TDREVRLGRN327 GVEEIKRHLF337 FKNDQWAWET347 LRDTVAPVVP357 DLSSDIDTSN 367 FDDLEEETFP382 IPKAFVGNQL392 PFVGFTYYSN402 RRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4TW or .4TW2 or .4TW3 or :34TW;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.122
GLY83
4.557
ARG84
3.609
GLY85
3.526
ALA86
3.224
PHE87
2.745
GLY88
3.386
GLU89
3.674
VAL90
3.558
ALA103
3.545
LYS105
3.033
LEU106
4.852
|
|||||
| Ligand Name: Cis-4-Amino-N-(7-Chloro-1-Oxo-1,2-Dihydroisoquinolin-6-Yl)cyclohexanecarboxamide | Ligand Info | |||||
| Structure Description | X-Ray Co-structure of Rho-Associated Protein Kinase (ROCK1) with a potent 2H-isoquinolin-1-one inhibitor | PDB:3NCZ | ||||
| Method | X-ray diffraction | Resolution | 3.00 Å | Mutation | No | [12] |
| PDB Sequence |
HMSFETRFEK
13 MDNLLRDPKS23 EVNSDCLLDG33 LDALVYDLDF43 PALRKNKNID53 NFLSRYKDTI 63 NKIRDLRMKA73 EDYEVVKVIG83 RGAFGEVQLV93 RHKSTRKVYA103 MKLLSKFEMI 113 KRSDSAFFWE123 ERDIMAFANS133 PWVVQLFYAF143 QDDRYLYMVM153 EYMPGGDLVN 163 LMSNYDVPEK173 WARFYTAEVV183 LALDAIHSMG193 FIHRDVKPDN203 MLLDKSGHLK 213 LADFGTCMKM223 NKEGMVRCDT233 AVGTPDYISP243 EVLKSQGGDG253 YYGRECDWWS 263 VGVFLYEMLV273 GDTPFYADSL283 VGTYSKIMNH293 KNSLTFPDDN303 DISKEAKNLI 313 CAFLTDREVR323 LGRNGVEEIK333 RHLFFKNDQW343 AWETLRDTVA353 PVVPDLSSDI 363 DTSNFDDLEE373 DKGEEETFPI383 PKAFVGNQLP393 FVGFTYYSN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3NC or .3NC2 or .3NC3 or :33NC;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:90 or .A:103 or .A:105 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:200 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| Ligand Name: (2R)-N-(3-cyanophenyl)-2-{3-[(5-methyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)carbamoyl]phenyl}pyrrolidine-1-carboxamide | Ligand Info | |||||
| Structure Description | X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR | PDB:5WNH | ||||
| Method | X-ray diffraction | Resolution | 3.10 Å | Mutation | No | [13] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEGE377 EETFPIPKAF387 VGNQLPFVGF397 TYYS
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .B5G or .B5G2 or .B5G3 or :3B5G;style chemicals stick;color identity;select .A:82 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:117 or .A:120 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.453
ARG84
3.714
GLY85
3.592
ALA86
3.535
PHE87
2.809
GLY88
3.694
GLU89
3.857
VAL90
3.435
ALA103
3.607
LYS105
2.812
LEU106
4.864
LEU107
3.540
ASP117
2.932
PHE120
3.509
|
|||||
| Ligand Name: 2-Fluoro-N-[4-(Pyridin-4-Yl)-1,3-Thiazol-2-Yl]benzamide | Ligand Info | |||||
| Structure Description | ROCK 1 bound to thiazole inhibitor | PDB:4YVC | ||||
| Method | X-ray diffraction | Resolution | 3.20 Å | Mutation | No | [11] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKF 120 FWEERDIMAF130 ANSPWVVQLF140 YAFQDDRYLY150 MVMEYMPGGD160 LVNLMSNYDV 170 PEKWARFYTA180 EVVLALDAIH190 SMGFIHRDVK200 PDNMLLDKSG210 HLKLADFGTC 220 MKMNKEGMVR230 CDTAVGTPDY240 ISPEVLKSQG250 GDGYYGRECD260 WWSVGVFLYE 270 MLVGDTPFYA280 DSLVGTYSKI290 MNHKNSLTFP300 DDNDISKEAK310 NLICAFLTDR 320 EVRLGRNGVE330 EIKRHLFFKN340 DQWAWETLRD350 TVAPVVPDLS360 SDIDTSNFDD 370 LETFPIPKAF387 VGNQLPFVGF397 TYYSNRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4KH or .4KH2 or .4KH3 or :34KH;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:87 or .A:90 or .A:103 or .A:105 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| Ligand Name: 2-[3-(Methylsulfonylamino)phenyl]-~{n}-[4-(1~{h}-Pyrrolo[2,3-B]pyridin-3-Yl)-1,3-Thiazol-2-Yl]ethanamide | Ligand Info | |||||
| Structure Description | ROCK 1 bound to azaindole thiazole inhibitor | PDB:5KKS | ||||
| Method | X-ray diffraction | Resolution | 3.30 Å | Mutation | No | [8] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSQGGDGYY255 GRECDWWSVG 265 VFLYEMLVGD275 TPFYADSLVG285 TYSKIMNHKN295 SLTFPDDNDI305 SKEAKNLICA 315 FLTDREVRLG325 RNGVEEIKRH335 LFFKNDQWAW345 ETLRDTVAPV355 VPDLSSDIDT 365 SNFDDLEEET380 FPIPKAFVGN390 QLPFVGFTYY400 SNRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6U1 or .6U12 or .6U13 or :36U1;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.802
GLY83
4.588
ARG84
3.536
GLY85
3.463
ALA86
3.092
PHE87
2.687
GLY88
3.115
GLU89
3.450
VAL90
3.321
ALA103
3.467
LYS105
3.230
LEU106
4.787
LEU107
4.190
|
|||||
| Ligand Name: N-[4-(2-aminopyridin-4-yl)-1,3-thiazol-2-yl]-2-(3-methoxyphenyl)acetamide | Ligand Info | |||||
| Structure Description | Crystal Structure of ROCK1 bound to an aminopyridine inhibitor | PDB:5UZJ | ||||
| Method | X-ray diffraction | Resolution | 3.30 Å | Mutation | No | [14] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKA 119 FFWEERDIMA129 FANSPWVVQL139 FYAFQDDRYL149 YMVMEYMPGG159 DLVNLMSNYD 169 VPEKWARFYT179 AEVVLALDAI189 HSMGFIHRDV199 KPDNMLLDKS209 GHLKLADFGT 219 CMKMNKEGMV229 RCDTAVGTPD239 YISPEVLKSG253 YYGRECDWWS263 VGVFLYEMLV 273 GDTPFYADSL283 VGTYSKIMNH293 KNSLTFPDDN303 DISKEAKNLI313 CAFLTDREVR 323 LGRNGVEEIK333 RHLFFKNDQW343 AWETLRDTVA353 PVVPDLSSDI363 DTSNFDDLEE 378 ETFPIPKAFV388 GNQLPFVGFT398 YYSNRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .8UV or .8UV2 or .8UV3 or :38UV;style chemicals stick;color identity;select .A:82 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.538
ARG84
3.978
GLY85
3.594
ALA86
3.686
PHE87
3.475
GLY88
3.239
GLU89
3.454
VAL90
3.297
ALA103
3.587
LYS105
3.285
LEU106
4.053
LEU107
3.673
|
|||||
| Ligand Name: 2-(3-Methoxyphenyl)-N-[4-(Pyridin-4-Yl)-1,3-Thiazol-2-Yl]acetamide | Ligand Info | |||||
| Structure Description | ROCK 1 bound to methoxyphenyl thiazole inhibitor | PDB:4YVE | ||||
| Method | X-ray diffraction | Resolution | 3.40 Å | Mutation | No | [11] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SDSAFFWEER125 DIMAFANSPW135 VVQLFYAFQD145 DRYLYMVMEY155 MPGGDLVNLM 165 SNYDVPEKWA175 RFYTAEVVLA185 LDAIHSMGFI195 HRDVKPDNML205 LDKSGHLKLA 215 DFGTCMKMNK225 EGMVRCDTAV235 GTPDYISPEV245 LKSGYYGREC259 DWWSVGVFLY 269 EMLVGDTPFY279 ADSLVGTYSK289 IMNHKNSLTF299 PDDNDISKEA309 KNLICAFLTD 319 REVRLGRNGV329 EEIKRHLFFK339 NDQWAWETLR349 DTVAPVVPDL359 SSDIDTSNFD 369 DLEETFPIPK385 AFVGNQLPFV395 GFTYYSNRRY405
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4KK or .4KK2 or .4KK3 or :34KK;style chemicals stick;color identity;select .A:82 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.659
ARG84
4.012
GLY85
3.362
ALA86
3.619
PHE87
3.254
GLY88
3.293
GLU89
3.584
VAL90
3.383
ALA103
3.596
LYS105
2.815
LEU106
4.179
LEU107
3.605
|
|||||
| Ligand Name: N-[(1S)-2-hydroxy-1-phenylethyl]-3-methoxy-4-(1H-pyrazol-4-yl)benzamide | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE 1 (ROCK1) IN COMPLEX WITH A PHENYLPYRAZOLE AMIDE INHIBITOR | PDB:7JOU | ||||
| Method | X-ray diffraction | Resolution | 3.32 Å | Mutation | No | [15] |
| PDB Sequence |
TRFEKMDNLL
18 RDPKSEVNSD28 CLLDGLDALV38 YDLDFPALRK48 NKNIDNFLSR58 YKDTINKIRD 68 LRMKAEDYEV78 VKVIGRGAFG88 EVQLVRHKST98 RKVYAMKLLS108 KFEMIKRSDS 118 AFFWEERDIM128 AFANSPWVVQ138 LFYAFQDDRY148 LYMVMEYMPG158 GDLVNLMSNY 168 DVPEKWARFY178 TAEVVLALDA188 IHSMGFIHRD198 VKPDNMLLDK208 SGHLKLADFG 218 TCMKMNKEGM228 VRCDTAVGTP238 DYISPEVLKS248 QGGDGYYGRE258 CDWWSVGVFL 268 YEMLVGDTPF278 YTYSKIMNHK294 NSLTFPDDND304 ISKEAKNLIC314 AFLTDREVRL 324 GRNGVEEIKR334 HLFFKNDQWA344 WETLRDTVAP354 VVPDLSSDID364 TSNFDDLEED 374 KGEEETFPIP384 KAFVGNQLPF394 VGFTYYSN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .VFS or .VFS2 or .VFS3 or :3VFS;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:107 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
3.540
GLY83
3.987
ARG84
3.254
GLY85
3.065
ALA86
3.482
PHE87
4.916
GLY88
3.552
GLU89
3.511
VAL90
3.623
ALA103
3.349
LYS105
3.113
|
|||||
| Ligand Name: N~1~-[2-(1h-Indazol-5-Yl)pyrido[3,4-D]pyrimidin-4-Yl]-2-Methylpropane-1,2-Diamine | Ligand Info | |||||
| Structure Description | Crystal Structure of ROCK 1 bound to YB-15-QD37 | PDB:4W7P | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [16] |
| PDB Sequence |
SFETRFEKMD
15 NLLRDPKSEV25 NSDCLLDGLD35 ALVYDLDFPA45 LRKNKNIDNF55 LSRYKDTINK 65 IRDLRMKAED75 YEVVKVIGRG85 AFGEVQLVRH95 KSTRKVYAMK105 LLSKFEMIKR 115 SFFWEERDIM128 AFANSPWVVQ138 LFYAFQDDRY148 LYMVMEYMPG158 GDLVNLMSNY 168 DVPEKWARFY178 TAEVVLALDA188 IHSMGFIHRD198 VKPDNMLLDK208 SGHLKLADFG 218 TCMKMNKEGM228 VRCDTAVGTP238 DYISPEVLKS248 DGYYGRECDW261 WSVGVFLYEM 271 LVGDTPFYAD281 SLVGTYSKIM291 NHKNSLTFPD301 DNDISKEAKN311 LICAFLTDRE 321 VRLGRNGVEE331 IKRHLFFKND341 QWAWETLRDT351 VAPVVPDLSS361 DIDTSNFDDL 371 EETFPIPKAF387 VGNQLPFVGF397 TYYSNRRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3J7 or .3J72 or .3J73 or :33J7;style chemicals stick;color identity;select .A:82 or .A:83 or .A:90 or .A:92 or .A:103 or .A:105 or .A:124 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:160 or .A:202 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| Ligand Name: 1-[(1r)-1-(3-Methoxyphenyl)ethyl]-3-(4-Pyridin-4-Yl-1,3-Thiazol-2-Yl)urea | Ligand Info | |||||
| Structure Description | Human Rho-associated protein kinase 1 (ROCK 1) in COMPLEX WITH RKI1342 | PDB:3TV7 | ||||
| Method | X-ray diffraction | Resolution | 2.75 Å | Mutation | No | [17] |
| PDB Sequence |
TRFEKMDNLL
18 RDPKSEVNSD28 CLLDGLDALV38 YDLDFPALRK48 NKNIDNFLSR58 YKDTINKIRD 68 LRMKAEDYEV78 VKVIGRGAFG88 EVQLVRHKST98 RKVYAMKLLS108 KFEMIKRSDS 118 AFFWEERDIM128 AFANSPWVVQ138 LFYAFQDDRY148 LYMVMEYMPG158 GDLVNLMSNY 168 DVPEKWARFY178 TAEVVLALDA188 IHSMGFIHRD198 VKPDNMLLDK208 SGHLKLADFG 218 TCMKMNKEGM228 VRCDTAVGTP238 DYISPEVLKS248 QGGDGYYGRE258 CDWWSVGVFL 268 YEMLVGDTPF278 YADSLVGTYS288 KIMNHKNSLT298 FPDDNDISKE308 AKNLICAFLT 318 DREVRLGRNG328 VEEIKRHLFF338 KNDQWAWETL348 RDTVAPVVPD358 LSSDIDTSNF 368 DDLEEDKGEE378 ETFPIPKAFV388 GNQLPFVGFT398 YYSN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .07Q or .07Q2 or .07Q3 or :307Q;style chemicals stick;color identity;select .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:103 or .A:105 or .A:106 or .A:107 or .A:120 or .A:124 or .A:128 or .A:137 or .A:153 or .A:154 or .A:155 or .A:156 or .A:203 or .A:205 or .A:215 or .A:216 or .A:368; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE82
4.225
GLY83
4.364
ARG84
3.984
GLY85
3.135
ALA86
4.816
PHE87
3.343
GLY88
3.236
GLU89
3.689
VAL90
3.610
ALA103
3.509
LYS105
2.983
LEU106
4.210
LEU107
3.929
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | The structure of dimeric ROCK I reveals the mechanism for ligand selectivity. J Biol Chem. 2006 Jan 6;281(1):260-8. | ||||
| REF 2 | Fragment-based and structure-guided discovery and optimization of Rho kinase inhibitors. J Med Chem. 2012 Mar 8;55(5):2474-8. | ||||
| REF 3 | RKI-1447 is a potent inhibitor of the Rho-associated ROCK kinases with anti-invasive and antitumor activities in breast cancer. Cancer Res. 2012 Oct 1;72(19):5025-34. | ||||
| REF 4 | Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure. EMBO J. 2008 Dec 3;27(23):3175-85. | ||||
| REF 5 | Identification of Selective Dual ROCK1 and ROCK2 Inhibitors Using Structure-Based Drug Design. J Med Chem. 2018 Dec 27;61(24):11074-11100. | ||||
| REF 6 | Novel mechanism of Rho kinase selectivity: beyond the ATP pocket | ||||
| REF 7 | Novel mechanism of Rho kinase selectivity: beyond the ATP pocket | ||||
| REF 8 | ROCK inhibitors 3: Design, synthesis and structure-activity relationships of 7-azaindole-based Rho kinase (ROCK) inhibitors. doi:10.1016/j.bmcl.2018.06.040. | ||||
| REF 9 | ROCK inhibitors 2. Improving potency, selectivity and solubility through the application of rationally designed solubilizing groups. Bioorg Med Chem Lett. 2018 Aug 15;28(15):2616-2621. | ||||
| REF 10 | Novel mechanism of Rho kinase selectivity: beyond the ATP pocket | ||||
| REF 11 | Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors. J Med Chem. 2015 Jun 25;58(12):5028-37. | ||||
| REF 12 | Substituted 2H-isoquinolin-1-ones as potent Rho-kinase inhibitors: part 2, optimization for blood pressure reduction in spontaneously hypertensive rats. Bioorg Med Chem Lett. 2010 Sep 1;20(17):5153-6. | ||||
| REF 13 | Novel mechanism of Rho kinase selectivity: beyond the ATP pocket | ||||
| REF 14 | ROCK inhibitors 3: Design, synthesis and structure-activity relationships of 7-azaindole-based Rho kinase (ROCK) inhibitors. Bioorg Med Chem Lett. 2018 Aug 15;28(15):2622-2626. | ||||
| REF 15 | Discovery of a phenylpyrazole amide ROCK inhibitor as a tool molecule for in vivo studies. Bioorg Med Chem Lett. 2020 Nov 1;30(21):127495. | ||||
| REF 16 | Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension. Bioorg Med Chem Lett. 2014 Oct 15;24(20):4812-7. | ||||
| REF 17 | Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2). Medchemcomm. 2012 Jun 1;3(6):699-709. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.