Structure of PDB 1iei Chain A Binding Site BS02
Receptor Information
>1iei Chain A (length=315) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN
ENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLK
LDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDE
GLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQ
SKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIR
FPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL
LSCTSHKDYPFHEEF
Ligand information
Ligand ID
ZES
InChI
InChI=1S/C17H11BrClFN2O4/c18-10-2-1-9(13(20)5-10)7-22-16(25)12-4-3-11(19)6-14(12)21(17(22)26)8-15(23)24/h1-6H,7-8H2,(H,23,24)
InChIKey
SXONDGSPUVNZLO-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
OC(=O)CN1C(=O)N(Cc2ccc(Br)cc2F)C(=O)c3ccc(Cl)cc13
OpenEye OEToolkits 1.5.0
c1cc2c(cc1Cl)N(C(=O)N(C2=O)Cc3ccc(cc3F)Br)CC(=O)O
ACDLabs 10.04
Brc1ccc(c(F)c1)CN3C(=O)c2c(cc(Cl)cc2)N(C3=O)CC(=O)O
Formula
C17 H11 Br Cl F N2 O4
Name
[3-(4-BROMO-2-FLUORO-BENZYL)-7-CHLORO-2,4-DIOXO-3,4-DIHYDRO-2H-QUINAZOLIN-1-YL]-ACETIC ACID
ChEMBL
CHEMBL10413
DrugBank
DB02132
ZINC
ZINC000000596737
PDB chain
1iei Chain A Residue 351 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1iei
The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
W20 V47 Y48 H110 W111 T113 F122 C298 A299 L300 Y309
Binding residue
(residue number reindexed from 1)
W20 V47 Y48 H110 W111 T113 F122 C298 A299 L300 Y309
Annotation score
1
Binding affinity
MOAD
: ic50=44nM
BindingDB: IC50=8nM
Enzymatic activity
Catalytic site (original residue number in PDB)
D43 Y48 K77 H110
Catalytic site (residue number reindexed from 1)
D43 Y48 K77 H110
Enzyme Commision number
1.1.1.21
: aldose reductase.
1.1.1.300
: NADP-retinol dehydrogenase.
1.1.1.372
: D/L-glyceraldehyde reductase.
1.1.1.54
: allyl-alcohol dehydrogenase.
Gene Ontology
Molecular Function
GO:0001758
retinal dehydrogenase activity
GO:0004032
aldose reductase (NADPH) activity
GO:0005515
protein binding
GO:0009055
electron transfer activity
GO:0016491
oxidoreductase activity
GO:0036130
prostaglandin H2 endoperoxidase reductase activity
GO:0043795
glyceraldehyde oxidoreductase activity
GO:0047655
allyl-alcohol dehydrogenase activity
GO:0047939
L-glucuronate reductase activity
GO:0047956
glycerol dehydrogenase (NADP+) activity
GO:0052650
all-trans-retinol dehydrogenase (NADP+) activity
Biological Process
GO:0001523
retinoid metabolic process
GO:0002070
epithelial cell maturation
GO:0003091
renal water homeostasis
GO:0005975
carbohydrate metabolic process
GO:0006629
lipid metabolic process
GO:0006693
prostaglandin metabolic process
GO:0006700
C21-steroid hormone biosynthetic process
GO:0019853
L-ascorbic acid biosynthetic process
GO:0035809
regulation of urine volume
GO:0042572
retinol metabolic process
GO:0043066
negative regulation of apoptotic process
GO:0044597
daunorubicin metabolic process
GO:0044598
doxorubicin metabolic process
GO:0046370
fructose biosynthetic process
GO:0071475
cellular hyperosmotic salinity response
GO:0072205
metanephric collecting duct development
Cellular Component
GO:0005615
extracellular space
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005739
mitochondrion
GO:0005829
cytosol
GO:0070062
extracellular exosome
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1iei
,
PDBe:1iei
,
PDBj:1iei
PDBsum
1iei
PubMed
11914486
UniProt
P15121
|ALDR_HUMAN Aldo-keto reductase family 1 member B1 (Gene Name=AKR1B1)
[
Back to BioLiP
]