Structure of PDB 1k8c Chain A Binding Site BS01

Receptor Information
>1k8c Chain A (length=317) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYG
NEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADL
KVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKA
LEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKL
IEFAQKAGVTITAYSSFGPQSFVNQGRALNTPTLFAHDTIKAIAAKYNKT
PAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKLDI
GLRFNDPWDWDNIPIFV
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 chain1k8c Chain A Residue 1350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure 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]
PDB1k8c The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		G22 C23 W24 D47 Y52 H114 Q191 Y217 F220 Q223 S224 A257 I272 P273 K274 S275 N276 R280 N284
Binding residue
(residue number reindexed from 1)		G19 C20 W21 D44 Y49 H111 Q188 Y214 F217 Q220 S221 A252 I267 P268 K269 S270 N271 R275 N279
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D47 Y52 K81 H114
Catalytic site (residue number reindexed from 1) D44 Y49 K78 H111
Enzyme Commision number 1.1.1.307: D-xylose reductase [NAD(P)H].
Gene Ontology
Molecular Function
GO:0004032 aldose reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0032866 D-xylose reductase (NADPH) activity
Biological Process
GO:0042732 D-xylose metabolic process
GO:0042843 D-xylose catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1k8c, PDBe:1k8c, PDBj:1k8c
PDBsum1k8c
PubMed12102621
UniProtO74237|XYL1_CANTE NAD(P)H-dependent D-xylose reductase (Gene Name=XYL1)

[Back to BioLiP]