Structure of PDB 1ae4 Chain A Binding Site BS01

Receptor Information
>1ae4 Chain A (length=324) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAIKYALTVGYRHIDCAAIYG
NELEIGEALTETVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLAD
LQLEYLDLYLMHWPYAFERGDNPFPKNADGTIRYDATHYKDTWKALEALV
AKGLVRALGLSNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQ
ARGLEVTAYSPLGSSDRAWRDPNEPVLLEEPVVQALAEKYNRSPAQILLR
WQVQRKVICIPKSVTPSRIPQNIQVFDFTFSPEEMKQLDALNKNLRFIVP
MLTVDGKRVPRDAGHPLYPFNDPY
Ligand information
Ligand IDNAP
InChIInChI=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)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyXJLXINKUBYWONI-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
FormulaC21 H28 N7 O17 P3
NameNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
ChEMBLCHEMBL295069
DrugBankDB03461
ZINC
PDB chain1ae4 Chain A Residue 350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ae4 Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G20 S211 S215 S264
Binding residue
(residue number reindexed from 1)		G19 S210 S214 S263
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D45 Y50 K80 H113
Catalytic site (residue number reindexed from 1) D44 Y49 K79 H112
Enzyme Commision number 1.1.1.19: glucuronate reductase.
1.1.1.2: alcohol dehydrogenase (NADP(+)).
1.1.1.20: glucuronolactone reductase.
1.1.1.372: D/L-glyceraldehyde reductase.
1.1.1.54: allyl-alcohol dehydrogenase.
1.6.-.-
Gene Ontology
Molecular Function
GO:0004032 aldose reductase (NADPH) activity
GO:0004745 all-trans-retinol dehydrogenase (NAD+) activity
GO:0008106 alcohol dehydrogenase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0047655 allyl-alcohol dehydrogenase activity
GO:0047939 L-glucuronate reductase activity
GO:0047941 glucuronolactone reductase activity
GO:0047956 glycerol dehydrogenase (NADP+) activity
GO:0160163 S-nitrosoglutathione reductase (NADPH) activity
GO:1990002 methylglyoxal reductase (NADPH) (acetol producing) activity
Biological Process
GO:0006629 lipid metabolic process
GO:0019853 L-ascorbic acid biosynthetic process
GO:0042840 D-glucuronate catabolic process
GO:0046185 aldehyde catabolic process
GO:0110095 cellular detoxification of aldehyde
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016324 apical plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ae4, PDBe:1ae4, PDBj:1ae4
PDBsum1ae4
PubMed9329083
UniProtP50578|AK1A1_PIG Aldo-keto reductase family 1 member A1 (Gene Name=AKR1A1)

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