Structure of PDB 1az2 Chain A

Receptor sequence
>1az2A (length=314) Species: 9606 (Homo sapiens) [Search protein sequence]
SRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNE
NEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKL
DYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEG
LVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQS
KGIVVTAYSPLGSPDRPYAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRF
PMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVAALL
SCTSHKDYPFHEEF
3D structure
PDB1az2 The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D43 Y48 K77 H110
Catalytic site (residue number reindexed from 1) D42 Y47 K76 H109
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAP A G18 T19 W20 K21 D43 Y48 H110 Q183 Y209 S210 L212 S214 P215 D216 L228 A245 I260 K262 S263 V264 T265 R268 N272 G17 T18 W19 K20 D42 Y47 H109 Q182 Y208 S209 L211 S213 P214 D215 L227 A244 I259 K261 S262 V263 T264 R267 N271
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:1az2, PDBe:1az2, PDBj:1az2
PDBsum1az2
PubMed9405046
UniProtP15121|ALDR_HUMAN Aldo-keto reductase family 1 member B1 (Gene Name=AKR1B1)

[Back to BioLiP]