Structure of PDB 4oaq Chain A Binding Site BS01

Receptor Information
>4oaq Chain A (length=365) Species: 5480 (Candida parapsilosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KAVPDKFQGFAVSDPKNWNRPKLASYERKQINPHDVVLKNEVCGLCYSDI
HTLSAGWQPLQRDNLVVGHEIIGEVIAVGDEVTEFKVGDRVGIGAASSSC
RSCQRCDSDNEQYCKQGAATYNSKDVRSNNYVTQGGYSSHSIADEKFVFA
IPEDLPSSYGAPLMCAGITVFSPLIRNLGLDARGKNVGIIGIGGLGHLAL
QFANAMGANVTAFSRSSSKKEQAMKLGAHDFVATGEDKTWYKNYDDHFDF
ILNCASGIDGLNLSEYLSTLKVDKKFVSVGLPPSEDKFEVSPFTFLQQGA
SFGSSLLGSKTEVKEMLNLAAKHNVRPMIEEVPISEENCAKALDRCHAGD
VRYRFVFTDFDKAFA
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/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/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[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)C1=CN(C=CC1)[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 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain4oaq Chain A Residue 401 [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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PDB4oaq Expression, purification, crystallization and preliminary X-ray diffraction analysis of carbonyl reductase from Candida parapsilosis ATCC 7330.
Resolution1.858 Å
Binding residue
(original residue number in PDB)		C48 Y49 S50 W59 C167 T171 I194 G195 G196 L197 S216 R217 K221 A257 S258 G259 D261 V281 G282 L283 L308 L309 R356
Binding residue
(residue number reindexed from 1)		C46 Y47 S48 W57 C165 T169 I192 G193 G194 L195 S214 R215 K219 A255 S256 G257 D259 V279 G280 L281 L306 L307 R354
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) C48 Y49 S50 H53 H71 E72 C102 C105 C108 C116 C167
Catalytic site (residue number reindexed from 1) C46 Y47 S48 H51 H69 E70 C100 C103 C106 C114 C165
Enzyme Commision number 1.1.1.195: cinnamyl-alcohol dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008106 alcohol dehydrogenase (NADP+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0006066 alcohol metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4oaq, PDBe:4oaq, PDBj:4oaq
PDBsum4oaq
PubMed
UniProtM4VRJ6

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