Structure of PDB 1hqt Chain A Binding Site BS01

Receptor Information

>1hqt Chain A (length=324) Species: 9823 (Sus scrofa)

AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAIKYALTVGYRHIDCAAIFG
NELEIGEALQETVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLAD
LQLEYLDLYLMHWPYAFERGDNPFPKNADGTIRYDATHYKDTWKALEALV
AKGLVRALGLSNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQ
ARGLEVTAYSPLGSSDRAWRDPNEPVLLEEPVVQALAEKYNRSPAQILLR
WQVQRKVICIPKSVTPSRIPQNIQVFDFTFSPEEMKQLDALNKNLRFIVP
MLTVDGKRVPRDAGHPLYPFNDPY

Ligand information

• Ligand ID: NAP
• InChI: InChI=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
• InChIKey: XJLXINKUBYWONI-NNYOXOHSSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: c1cc(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 3.341: NC(=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 3.341: NC(=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 1.5.0: c1cc(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
• Formula: C21 H28 N7 O17 P3
• Name: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
  2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
• ChEMBL: CHEMBL295069
• DrugBank: DB03461
• PDB chain: 1hqt Chain A Residue 350

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1hqt The Crystal Structure of an Aldehyde Reductase Y50F Mutant-NADP Complex and its Implications for Substrate Binding
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): G20 T21 W22 D45 F50 K80 H113 S162 Q184 Y210 S211 P212 L213 S215 S216 A246 I261 K263 S264 V265 T266 R269 N273
• Binding residue (residue number reindexed from 1): G19 T20 W21 D44 F49 K79 H112 S161 Q183 Y209 S210 P211 L212 S214 S215 A245 I260 K262 S263 V264 T265 R268 N272
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): D45 F50 K80 H113
• Catalytic site (residue number reindexed from 1): D44 F49 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

External links

• PDB: RCSB:1hqt, PDBe:1hqt, PDBj:1hqt
• PDBsum: 1hqt
• PubMed: 11306083
• UniProt: P50578|AK1A1_PIG Aldo-keto reductase family 1 member A1 (Gene Name=AKR1A1)