Structure of PDB 4h8n Chain A Binding Site BS01

Receptor Information
>4h8n Chain A (length=303) Species: 5480 (Candida parapsilosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLLPKTFRTKSGKEISIALGTGTKWKQAQTINDVSTELVDNILLGLKLGF
RHIDTAEAYNTQKEVGEALKRTDVPREDIWVTTKYSPGWGSIKAYSKSPS
DSIDKALAQLGVDYVDLFLIHSPFFTTEQTHGYTLEQAWEALVEAKKAGK
VREIGISNAAIPHLEKLFAASPSPEYYPVVNQIEFHPFLQNQSKNIVRFC
QEHGILVEAFSPLAPLARVETNALAETLKRLAEKYKKTEAQVLLRYTLQR
GILPVTTSSKESRLKESLNLFDFELTDEEVNEINKIGDANPYRAFFHEQF
KDL
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 chain4h8n Chain A Residue 3001 [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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PDB4h8n Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding
Resolution1.8 Å
Binding residue
(original residue number in PDB)		G24 G26 T27 K28 D58 Y63 H125 Q186 F214 S215 P216 L217 A221 V259 T260 T261 S262 S263 K264 R267
Binding residue
(residue number reindexed from 1)		G20 G22 T23 K24 D54 Y59 H121 Q182 F210 S211 P212 L213 A217 V255 T256 T257 S258 S259 K260 R263
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D58 Y63 K88 H125
Catalytic site (residue number reindexed from 1) D54 Y59 K84 H121
Enzyme Commision number 1.1.1.-
1.1.1.358: 2-dehydropantolactone reductase.
Gene Ontology
Molecular Function
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016652 oxidoreductase activity, acting on NAD(P)H as acceptor
GO:0036441 2-dehydropantolactone reductase activity
GO:0047011 2-dehydropantolactone reductase (A-specific) activity
Biological Process
GO:0042180 cellular ketone metabolic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4h8n, PDBe:4h8n, PDBj:4h8n
PDBsum4h8n
PubMed23828603
UniProtQ76L36|CPRC2_CANPA NADPH-dependent conjugated polyketone reductase C2 (Gene Name=cpr-c2)

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