Structure of PDB 3vzs Chain B Binding Site BS02

Receptor Information
>3vzs Chain B (length=249) Species: 381666 (Cupriavidus necator H16) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HHGSTQRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQ
QKALGFDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVF
RKMTRADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQ
FGQTNYSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQD
VLDKIVATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG
Ligand information
Ligand IDCAA
InChIInChI=1S/C25H40N7O18P3S/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32/h11-12,14,18-20,24,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)/t14-,18-,19-,20+,24-/m1/s1
InChIKeyOJFDKHTZOUZBOS-CITAKDKDSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
CACTVS 3.341CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
OpenEye OEToolkits 1.5.0CC(=O)CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
ACDLabs 10.04O=C(C)CC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC25 H40 N7 O18 P3 S
NameACETOACETYL-COENZYME A
ChEMBL
DrugBankDB03059
ZINCZINC000096014521
PDB chain3vzs Chain B Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3vzs Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics
Resolution2.14 Å
Binding residue
(original residue number in PDB)		D94 Q147 F148 Q150 Y153 G184 Y185 R195
Binding residue
(residue number reindexed from 1)		D97 Q150 F151 Q153 Y156 G187 Y188 R198
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N112 S140 Y153 K157
Catalytic site (residue number reindexed from 1) N115 S143 Y156 K160
Enzyme Commision number 1.1.1.36: acetoacetyl-CoA reductase.
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0018454 acetoacetyl-CoA reductase activity
Biological Process
GO:0042619 poly-hydroxybutyrate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3vzs, PDBe:3vzs, PDBj:3vzs
PDBsum3vzs
PubMed23913421
UniProtP14697|PHAB_CUPNH Acetoacetyl-CoA reductase (Gene Name=phaB)

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