Structure of PDB 5f38 Chain B Binding Site BS01

Receptor Information
>5f38 Chain B (length=391) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDE
VIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVNKVCGSGLKSVALAAQ
AIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDGLM
CATHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEI
VPVNVVTKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTAGNASGIND
GAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQ
LAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIG
ASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL
Ligand information
Ligand IDCOZ
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-HDCXRZRFSA-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
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
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
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
ChEMBL
DrugBank
ZINCZINC000008215426
PDB chain5f38 Chain B 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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PDB5f38 Crystal structure of a thiolase from Escherichia coli at 1.8 angstrom resolution.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		C88 L149 K221 F236 A244 S248 A319 F320 H349
Binding residue
(residue number reindexed from 1)		C88 L149 K219 F234 A242 S246 A317 F318 H347
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) C88 H349 C379 G381
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
GO:0042802 identical protein binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0043442 acetoacetic acid catabolic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0032991 protein-containing complex

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5f38, PDBe:5f38, PDBj:5f38
PDBsum5f38
PubMed27380370
UniProtP76461|ATOB_ECOLI Acetyl-CoA acetyltransferase (Gene Name=atoB)

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