Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T01597 | Target Info | |||
| Target Name | Catalase (CAT) | ||||
| Synonyms | Human catalase | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | CAT | ||||
| Biochemical Class | Peroxide acceptor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | NADPH | Ligand Info | |||
| Canonical SMILES | C1C=CN(C=C1C(=O)N)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OCC3C(C(C(O3)N4C=NC5=C(N=CN=C54)N)OP(=O)(O)O)O)O)O | ||||
| InChI | 1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 | ||||
| InChIKey | ACFIXJIJDZMPPO-NNYOXOHSSA-N | ||||
| PubChem Compound ID | 5884 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 7P8W Human erythrocyte catalase cryoEM | ||||||
| Method | Electron microscopy | Resolution | 2.20 Å | Mutation | No | [1] |
| PDB Sequence |
SRDPASDQMQ
13 HWKEQRAAQK23 ADVLTTGAGN33 PVGDKLNVIT43 VGPRGPLLVQ53 DVVFTDEMAH 63 FDRERIPERV73 VHAKGAGAFG83 YFEVTHDITK93 YSKAKVFEHI103 GKKTPIAVRF 113 STVAGESGSA123 DTVRDPRGFA133 VKFYTEDGNW143 DLVGNNTPIF153 FIRDPILFPS 163 FIHSQKRNPQ173 THLKDPDMVW183 DFWSLRPESL193 HQVSFLFSDR203 GIPDGHRHMN 213 GYGSHTFKLV223 NANGEAVYCK233 FHYKTDQGIK243 NLSVEDAARL253 SQEDPDYGIR 263 DLFNAIATGK273 YPSWTFYIQV283 MTFNQAETFP293 FNPFDLTKVW303 PHKDYPLIPV 313 GKLVLNRNPV323 NYFAEVEQIA333 FDPSNMPPGI343 EASPDKMLQG353 RLFAYPDTHR 363 HRLGPNYLHI373 PVNCPYRARV383 ANYQRDGPMC393 MQDNQGGAPN403 YYPNSFGAPE 413 QQPSALEHSI423 QYSGEVRRFN433 TANDDNVTQV443 RAFYVNVLNE453 EQRKRLCENI 463 AGHLKDAQIF473 IQKKAVKNFT483 EVHPDYGSHI493 QALLDKYNAE503 KP |
|||||
|
|
PRO151
3.676
HIS194
2.494
PHE198
3.399
SER201
3.007
ASP202
4.488
ARG203
2.870
ASN213
2.902
TYR215
4.402
HIS235
3.551
LYS237
3.203
ILE242
4.034
GLN282
4.286
|
|||||
| PDB ID: 7VD9 2.29 A structure of the human catalase | ||||||
| Method | Electron microscopy | Resolution | 2.29 Å | Mutation | No | [2] |
| PDB Sequence |
SRDPASDQMQ
13 HWKEQRAAQK23 ADVLTTGAGN33 PVGDKLNVIT43 VGPRGPLLVQ53 DVVFTDEMAH 63 FDRERIPERV73 VHAKGAGAFG83 YFEVTHDITK93 YSKAKVFEHI103 GKKTPIAVRF 113 STVAGESGSA123 DTVRDPRGFA133 VKFYTEDGNW143 DLVGNNTPIF153 FIRDPILFPS 163 FIHSQKRNPQ173 THLKDPDMVW183 DFWSLRPESL193 HQVSFLFSDR203 GIPDGHRHMN 213 GYGSHTFKLV223 NANGEAVYCK233 FHYKTDQGIK243 NLSVEDAARL253 SQEDPDYGIR 263 DLFNAIATGK273 YPSWTFYIQV283 MTFNQAETFP293 FNPFDLTKVW303 PHKDYPLIPV 313 GKLVLNRNPV323 NYFAEVEQIA333 FDPSNMPPGI343 EASPDKMLQG353 RLFAYPDTHR 363 HRLGPNYLHI373 PVNCPYRARV383 ANYQRDGPMC393 MQDNQGGAPN403 YYPNSFGAPE 413 QQPSALEHSI423 QYSGEVRRFN433 TANDDNVTQV443 RAFYVNVLNE453 EQRKRLCENI 463 AGHLKDAQIF473 IQKKAVKNFT483 EVHPDYGSHI493 QALLDKYN
|
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|
|
PRO151
3.544
HIS194
2.543
PHE198
3.353
SER201
3.137
ASP202
4.366
ARG203
2.730
ASN213
3.065
TYR215
4.378
HIS235
3.733
LYS237
3.469
ILE242
4.394
|
|||||
| PDB ID: 1DGH HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [3] |
| PDB Sequence |
RDPASDQMQH
14 WKEQRAAQKA24 DVLTTGAGNP34 VGDKLNVITV44 GPRGPLLVQD54 VVFTDEMAHF 64 DRERIPERVV74 HAKGAGAFGY84 FEVTHDITKY94 SKAKVFEHIG104 KKTPIAVRFS 114 TVAGESGSAD124 TVRDPRGFAV134 KFYTEDGNWD144 LVGNNTPIFF154 IRDPILFPSF 164 IHSQKRNPQT174 HLKDPDMVWD184 FWSLRPESLH194 QVSFLFSDRG204 IPDGHRHMNG 214 YGSHTFKLVN224 ANGEAVYCKF234 HYKTDQGIKN244 LSVEDAARLS254 QEDPDYGIRD 264 LFNAIATGKY274 PSWTFYIQVM284 TFNQAETFPF294 NPFDLTKVWP304 HKDYPLIPVG 314 KLVLNRNPVN324 YFAEVEQIAF334 DPSNMPPGIE344 ASPDKMLQGR354 LFAYPDTHRH 364 RLGPNYLHIP374 VNCPYRARVA384 NYQRDGPMCM394 QDNQGGAPNY404 YPNSFGAPEQ 414 QPSALEHSIQ424 YSGEVRRFNT434 ANDDNVTQVR444 AFYVNVLNEE454 QRKRLCENIA 464 GHLKDAQIFI474 QKKAVKNFTE484 VHPDYGSHIQ494 ALLDKYN
|
|||||
|
|
PRO151
3.749
HIS194
2.603
PHE198
3.417
SER201
2.949
ASP202
4.713
ARG203
2.960
ASN213
3.025
TYR215
4.234
HIS235
3.422
LYS237
3.107
ILE242
4.006
GLN282
4.291
|
|||||
| PDB ID: 1DGB HUMAN ERYTHROCYTE CATALASE | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | No | [3] |
| PDB Sequence |
SRDPASDQMQ
13 HWKEQRAAQK23 ADVLTTGAGN33 PVGDKLNVIT43 VGPRGPLLVQ53 DVVFTDEMAH 63 FDRERIPERV73 VHAKGAGAFG83 YFEVTHDITK93 YSKAKVFEHI103 GKKTPIAVRF 113 STVAGESGSA123 DTVRDPRGFA133 VKFYTEDGNW143 DLVGNNTPIF153 FIRDPILFPS 163 FIHSQKRNPQ173 THLKDPDMVW183 DFWSLRPESL193 HQVSFLFSDR203 GIPDGHRHMN 213 GYGSHTFKLV223 NANGEAVYCK233 FHYKTDQGIK243 NLSVEDAARL253 SQEDPDYGIR 263 DLFNAIATGK273 YPSWTFYIQV283 MTFNQAETFP293 FNPFDLTKVW303 PHKDYPLIPV 313 GKLVLNRNPV323 NYFAEVEQIA333 FDPSNMPPGI343 EASPDKMLQG353 RLFAYPDTHR 363 HRLGPNYLHI373 PVNCPYRARV383 ANYQRDGPMC393 MQDNQGGAPN403 YYPNSFGAPE 413 QQPSALEHSI423 QYSGEVRRFN433 TANDDNVTQV443 RAFYVNVLNE453 EQRKRLCENI 463 AGHLKDAQIF473 IQKKAVKNFT483 EVHPDYGSHI493 QALLDKYN
|
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NDP or .NDP2 or .NDP3 or :3NDP;style chemicals stick;color identity;select .A:151 or .A:194 or .A:198 or .A:201 or .A:202 or .A:203 or .A:213 or .A:215 or .A:235 or .A:237 or .A:242 or .A:282 or .A:302 or .A:303 or .A:304 or .A:305 or .A:306 or .A:442 or .A:445 or .A:446 or .A:450 or .A:451; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PRO151
3.749
HIS194
2.790
PHE198
3.412
SER201
2.841
ASP202
4.463
ARG203
2.596
ASN213
2.725
TYR215
4.305
HIS235
3.662
LYS237
3.242
ILE242
4.121
|
|||||
| PDB ID: 1DGF HUMAN ERYTHROCYTE CATALASE | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [3] |
| PDB Sequence |
RDPASDQMQH
14 WKEQRAAQKA24 DVLTTGAGNP34 VGDKLNVITV44 GPRGPLLVQD54 VVFTDEMAHF 64 DRERIPERVV74 HAKGAGAFGY84 FEVTHDITKY94 SKAKVFEHIG104 KKTPIAVRFS 114 TVAGESGSAD124 TVRDPRGFAV134 KFYTEDGNWD144 LVGNNTPIFF154 IRDPILFPSF 164 IHSQKRNPQT174 HLKDPDMVWD184 FWSLRPESLH194 QVSFLFSDRG204 IPDGHRHMNG 214 YGSHTFKLVN224 ANGEAVYCKF234 HYKTDQGIKN244 LSVEDAARLS254 QEDPDYGIRD 264 LFNAIATGKY274 PSWTFYIQVM284 TFNQAETFPF294 NPFDLTKVWP304 HKDYPLIPVG 314 KLVLNRNPVN324 YFAEVEQIAF334 DPSNMPPGIE344 ASPDKMLQGR354 LFAYPDTHRH 364 RLGPNYLHIP374 VNCPYRARVA384 NYQRDGPMCM394 QDNQGGAPNY404 YPNSFGAPEQ 414 QPSALEHSIQ424 YSGEVRRFNT434 ANDDNVTQVR444 AFYVNVLNEE454 QRKRLCENIA 464 GHLKDAQIFI474 QKKAVKNFTE484 VHPDYGSHIQ494 ALLDKYN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NDP or .NDP2 or .NDP3 or :3NDP;style chemicals stick;color identity;select .A:151 or .A:194 or .A:198 or .A:201 or .A:202 or .A:203 or .A:213 or .A:215 or .A:235 or .A:237 or .A:242 or .A:282 or .A:302 or .A:303 or .A:304 or .A:305 or .A:306 or .A:442 or .A:445 or .A:446 or .A:450 or .A:451; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PRO151
3.570
HIS194
2.632
PHE198
3.370
SER201
3.067
ASP202
4.512
ARG203
2.829
ASN213
2.589
TYR215
4.270
HIS235
3.479
LYS237
2.721
ILE242
4.348
|
|||||
| PDB ID: 1DGG HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [3] |
| PDB Sequence |
RDPASDQMQH
14 WKEQRAAQKA24 DVLTTGAGNP34 VGDKLNVITV44 GPRGPLLVQD54 VVFTDEMAHF 64 DRERIPERVV74 HAKGAGAFGY84 FEVTHDITKY94 SKAKVFEHIG104 KKTPIAVRFS 114 TVAGESGSAD124 TVRDPRGFAV134 KFYTEDGNWD144 LVGNNTPIFF154 IRDPILFPSF 164 IHSQKRNPQT174 HLKDPDMVWD184 FWSLRPESLH194 QVSFLFSDRG204 IPDGHRHMNG 214 YGSHTFKLVN224 ANGEAVYCKF234 HYKTDQGIKN244 LSVEDAARLS254 QEDPDYGIRD 264 LFNAIATGKY274 PSWTFYIQVM284 TFNQAETFPF294 NPFDLTKVWP304 HKDYPLIPVG 314 KLVLNRNPVN324 YFAEVEQIAF334 DPSNMPPGIE344 ASPDKMLQGR354 LFAYPDTHRH 364 RLGPNYLHIP374 VNCPYRARVA384 NYQRDGPMCM394 QDNQGGAPNY404 YPNSFGAPEQ 414 QPSALEHSIQ424 YSGEVRRFNT434 ANDDNVTQVR444 AFYVNVLNEE454 QRKRLCENIA 464 GHLKDAQIFI474 QKKAVKNFTE484 VHPDYGSHIQ494 ALLDKYN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NDP or .NDP2 or .NDP3 or :3NDP;style chemicals stick;color identity;select .A:151 or .A:194 or .A:198 or .A:201 or .A:202 or .A:203 or .A:213 or .A:215 or .A:235 or .A:237 or .A:242 or .A:282 or .A:302 or .A:303 or .A:304 or .A:305 or .A:306 or .A:442 or .A:443 or .A:445 or .A:446 or .A:450 or .A:451; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PRO151
3.769
HIS194
2.684
PHE198
3.229
SER201
2.980
ASP202
4.435
ARG203
2.869
ASN213
2.600
TYR215
4.386
HIS235
3.422
LYS237
3.325
ILE242
4.311
GLN282
4.203
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Interaction of human erythrocyte catalase with air-water interface in cryoEM. Microscopy (Oxf). 2022 Feb 18;71(Supplement_1):i51-i59. | ||||
| REF 2 | A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI. Nat Commun. 2021 Dec 14;12(1):7257. | ||||
| REF 3 | Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. | ||||
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