Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T70518 | Target Info | |||
| Target Name | S-nitrosoglutathione reductase (CBR1) | ||||
| Synonyms | ProstaglandinE(2) 9reductase; Prostaglandin 9ketoreductase; NADPHdependent carbonyl reductase 1; Carbonyl reductase [NADPH] 1; CBR1; 15hydroxyprostaglandin dehydrogenase [NADP(+)] | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | CBR1 | ||||
| Biochemical Class | Short-chain dehydrogenases reductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | NADP+ | Ligand Info | |||
| Canonical SMILES | C1=CC(=C[N+](=C1)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)C(=O)N | ||||
| InChI | 1S/C21H28N7O17P3/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/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/p+1/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 | ||||
| InChIKey | XJLXINKUBYWONI-NNYOXOHSSA-O | ||||
| PubChem Compound ID | 5886 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2PFG Crystal structure of human CBR1 in complex with BiGF2. | ||||||
| Method | X-ray diffraction | Resolution | 1.54 Å | Mutation | No | [1] |
| PDB Sequence |
GIHVALVTGG
12 NKGIGLAIVR22 DLCRLFSGDV32 VLTARDVTRG42 QAAVQQLQAE52 GLSPRFHQLD 62 IDDLQSIRAL72 RDFLRKEYGG82 LDVLVNNAGI92 AFKVADPTPF102 HIQAEVTMKT 112 NFFGTRDVTE123 LLPLIKPQGR133 VVNVSSIMSV143 RALKSCSPEL153 QQKFRSETIT 163 EEELVGLMNK173 FVEDTKKGVH183 QKEGWPSSAY193 GVTKIGVTVL203 SRIHARKLSE 213 QRKGDKILLN223 ACCPGWVRTD233 MAGPKATKSP243 EEGAETPVYL253 ALLPPDAEGP 263 HGQFVSEKRV273 EQW
|
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|
|
GLY11
3.267
GLY12
4.002
ASN13
2.780
LYS14
3.507
GLY15
3.337
ILE16
2.797
GLY17
4.365
ARG37
2.816
ASP38
4.674
ARG41
2.785
LEU61
3.354
ASP62
2.983
ILE63
2.980
ASP64
3.414
ASN89
2.741
ALA90
3.502
|
|||||
| PDB ID: 3BHJ Crystal structure of human Carbonyl Reductase 1 in complex with glutathione | ||||||
| Method | X-ray diffraction | Resolution | 1.77 Å | Mutation | No | [2] |
| PDB Sequence |
SGIHVALVTG
11 GNKGIGLAIV21 RDLCRLFSGD31 VVLTARDVTR41 GQAAVQQLQA51 EGLSPRFHQL 61 DIDDLQSIRA71 LRDFLRKEYG81 GLDVLVNNAG91 IAFKVADPTP101 FHIQAEVTMK 111 TNFFGTRDVC121 TELLPLIKPQ131 GRVVNVSSIM141 SVRALKSCSP151 ELQQKFRSET 161 ITEEELVGLM171 NKFVEDTKKG181 VHQKEGWPSS191 AYGVTKIGVT201 VLSRIHARKL 211 SEQRKGDKIL221 LNACCPGWVR231 TDMAGPKATK241 SPEEGAETPV251 YLALLPPDAE 261 GPHGQFVSEK271 RVEQW
|
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|
|
GLY11
3.243
GLY12
3.989
ASN13
2.745
LYS14
3.471
GLY15
3.460
ILE16
2.846
GLY17
4.355
ARG37
2.842
ASP38
4.603
ARG41
4.168
LEU61
3.434
ASP62
3.092
ILE63
3.003
ASP64
3.252
ASN89
2.726
ALA90
3.515
GLY91
3.557
|
|||||
| PDB ID: 3BHM Crystal structure of human Carbonyl Reductase 1 in complex with S-hydroxymethylglutathione | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [2] |
| PDB Sequence |
GIHVALVTGG
12 NKGIGLAIVR22 DLCRLFSGDV32 VLTARDVTRG42 QAAVQQLQAE52 GLSPRFHQLD 62 IDDLQSIRAL72 RDFLRKEYGG82 LDVLVNNAGI92 AFKVADPTPF102 HIQAEVTMKT 112 NFFGTRDVCT122 ELLPLIKPQG132 RVVNVSSIMS142 VRALKSCSPE152 LQQKFRSETI 162 TEEELVGLMN172 KFVEDTKKGV182 HQKEGWPSSA192 YGVTKIGVTV202 LSRIHARKLS 212 EQRKGDKILL222 NACCPGWVRT232 DMAGPKATKS242 PEEGAETPVY252 LALLPPDAEG 262 PHGQFVSEKR272 VEQW
|
|||||
|
|
GLY11
3.289
GLY12
4.041
ASN13
2.773
LYS14
3.425
GLY15
3.468
ILE16
2.860
GLY17
4.353
ARG37
2.827
ASP38
4.573
ARG41
4.290
LEU61
3.440
ASP62
3.079
ILE63
2.996
ASP64
3.332
ASN89
2.741
ALA90
3.488
GLY91
3.557
|
|||||
| PDB ID: 3BHI Crystal structure of human Carbonyl Reductase 1 in complex with NADP | ||||||
| Method | X-ray diffraction | Resolution | 2.27 Å | Mutation | No | [2] |
| PDB Sequence |
SGIHVALVTG
11 GNKGIGLAIV21 RDLCRLFSGD31 VVLTARDVTR41 GQAAVQQLQA51 EGLSPRFHQL 61 DIDDLQSIRA71 LRDFLRKEYG81 GLDVLVNNAG91 IAFKVADPTP101 FHIQAEVTMK 111 TNFFGTRDVC121 TELLPLIKPQ131 GRVVNVSSIM141 SVRALKSCSP151 ELQQKFRSET 161 ITEEELVGLM171 NKFVEDTKKG181 VHQKEGWPSS191 AYGVTKIGVT201 VLSRIHARKL 211 SEQRKGDKIL221 LNACCPGWVR231 TDMAGPKATK241 SPEEGAETPV251 YLALLPPDAE 261 GPHGQFVSEK271 RVEQW
|
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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 .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:37 or .A:38 or .A:41 or .A:61 or .A:62 or .A:63 or .A:64 or .A:89 or .A:90 or .A:91 or .A:92 or .A:112 or .A:113 or .A:137 or .A:138 or .A:139 or .A:193 or .A:197 or .A:227 or .A:228 or .A:229 or .A:230 or .A:232 or .A:233 or .A:234 or .A:235; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
GLY11
3.374
GLY12
4.090
ASN13
2.732
LYS14
3.123
GLY15
3.373
ILE16
2.751
GLY17
4.251
ARG37
2.834
ASP38
4.748
ARG41
2.798
LEU61
3.445
ASP62
2.784
ILE63
3.249
ASP64
3.594
ASN89
2.696
ALA90
3.506
GLY91
3.496
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. Org Biomol Chem. 2007 Oct 21;5(20):3363-7. | ||||
| REF 2 | Human carbonyl reductase 1 is an S-nitrosoglutathione reductase. J Biol Chem. 2008 Dec 19;283(51):35756-62. | ||||
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