Structure of PDB 2vu0 Chain A Binding Site BS01

Receptor Information
>2vu0 Chain A (length=391) Species: 350 (Zoogloea ramigera) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNE
VILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQ
QIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDA
FYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVP
FIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLND
GAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALE
RAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIG
ASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(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)[C@@H](O)C(=O)NCCC(=O)NCCS
OpenEye OEToolkits 1.5.0CC(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)[C@H](C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain2vu0 Chain A Residue 1393 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vu0 The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.
Resolution1.87 Å
Binding residue
(original residue number in PDB)		L148 H156 M157 R220 S227 M228 F235 A243 S247 F319 H348
Binding residue
(residue number reindexed from 1)		L147 H155 M156 R219 S226 M227 F234 A242 S246 F318 H347
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) C89 H348 C378 G380
Catalytic site (residue number reindexed from 1) C88 H347 C377 G379
Enzyme Commision number 2.3.1.9: acetyl-CoA C-acetyltransferase.
Gene Ontology
Molecular Function
GO:0003985 acetyl-CoA C-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
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:2vu0, PDBe:2vu0, PDBj:2vu0
PDBsum2vu0
PubMed19016856
UniProtP07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)

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