Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
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
CBR1_HUMAN
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: 1WMA      Crystal structure of human CBR1 in complex with Hydroxy-PP
Method X-ray diffraction Resolution 1.24 Å Mutation No [1]
PDB Sequence
SGIHVALVTG
11
GNKGIGLAIV
21
RDLCRLFSGD
31
VVLTARDVTR
41
GQAAVQQLQA
51

EGLSPRFHQL
61
DIDDLQSIRA
71
LRDFLRKEYG
81
GLDVLVNNAG
91
IAFKVADPTP
101

FHIQAEVTMK
111
TNFFGTRDVC
121
TELLPLIKPQ
131
GRVVNVSSIM
141
SVRALKSCSP
151

ELQQKFRSET
161
ITEEELVGLM
171
NKFVEDTKKG
181
VHQKEGWPSS
191
AYGVTKIGVT
201

VLSRIHARKL
211
SEQRKGDKIL
221
LNACCPGWVR
231
TDMAGPKATK
241
SPEEGAETPV
251

YLALLPPDAE
261
GPHGQFVSEK
271
RVEQW
Residue
Distance (Å)
GLY11
3.263
GLY12
3.964
ASN13
2.793
LYS14
3.435
GLY15
3.481
ILE16
2.853
GLY17
4.365
ARG37
2.800
ASP38
4.575
ARG41
4.128
LEU61
3.528
ASP62
2.968
ILE63
3.031
ASP64
3.400
ASN89
2.790
ALA90
3.539
GLY91
3.565
Residue
Distance (Å)
ILE92
3.574
THR112
3.849
VAL137
3.408
SER138
3.253
SER139
3.729
TYR193
2.686
LYS197
2.879
CYS226
3.752
PRO227
3.490
GLY228
3.021
TRP229
3.456
VAL230
2.862
THR232
2.667
ASP233
3.678
MET234
3.513
ALA235
3.628
PDB ID: 4Z3D      Human carbonyl reductase 1 with glutathione in a protective configuration
Method X-ray diffraction Resolution 1.80 Å Mutation No [2]
PDB Sequence
SSGIHVALVT
10
GGNKGIGLAI
20
VRDLCRLFSG
30
DVVLTARDVT
40
RGQAAVQQLQ
50

AEGLSPRFHQ
60
LDIDDLQSIR
70
ALRDFLRKEY
80
GGLDVLVNNA
90
GIAFKVADPT
100

PFHIQAEVTM
110
KTNFFGTRDV
120
CTELLPLIKP
130
QGRVVNVSSI
140
MSVRALKSCS
150

PELQQKFRSE
160
TITEEELVGL
170
MNKFVEDTKK
180
GVHQKEGWPS
190
SAYGVTKIGV
200

TVLSRIHARK
210
LSEQRKGDKI
220
LLNACCPGWV
230
RTDMAGPKAT
240
KSPEEGAETP
250

VYLALLPPDA
260
EGPHGQFVSE
270
KRVEQW
Residue
Distance (Å)
GLY11
3.299
GLY12
4.135
ASN13
2.790
LYS14
3.579
GLY15
3.490
ILE16
2.824
GLY17
4.312
ARG37
2.897
ASP38
4.699
ARG41
2.720
LEU61
3.411
ASP62
3.008
ILE63
3.015
ASP64
3.020
ASN89
2.734
ALA90
3.579
GLY91
3.529
Residue
Distance (Å)
ILE92
3.512
THR112
3.872
VAL137
3.549
SER138
3.182
SER139
3.745
TYR193
2.685
LYS197
2.904
CYS226
4.157
PRO227
3.588
GLY228
2.973
TRP229
3.534
VAL230
2.901
THR232
2.692
ASP233
3.659
MET234
3.501
ALA235
3.567
References  Top
REF 1 An unbiased cell morphology-based screen for new, biologically active small molecules. PLoS Biol. 2005 May;3(5):e128.
REF 2 Structural insights on the catalytic site protection of human carbonyl reductase 1 by glutathione. J Struct Biol. 2015 Oct;192(1):138-44.

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