Structure of PDB 1ah0 Chain A

Receptor sequence
>1ah0A (length=315) Species: 9823 (Sus scrofa) [Search protein sequence]
ASHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQN
ENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLK
LDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDE
GLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCK
SKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIR
FPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCAL
MSCASHKDYPFHEEY
3D structure
PDB1ah0 A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0001758 retinal dehydrogenase activity
GO:0004032 aldose reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0036130 prostaglandin H2 endoperoxidase reductase activity
GO:0047655 allyl-alcohol dehydrogenase activity
GO:0047956 glycerol dehydrogenase (NADP+) activity
GO:0052650 all-trans-retinol dehydrogenase (NADP+) activity
Biological Process
GO:0001523 retinoid metabolic process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0042572 retinol metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ah0, PDBe:1ah0, PDBj:1ah0
PDBsum1ah0
PubMed9195881
UniProtP80276|ALDR_PIG Aldo-keto reductase family 1 member B1 (Gene Name=AKR1B1)

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