Structure of PDB 5f38 Chain D

Receptor sequence
>5f38D (length=394) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ASMKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHV
DEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVNKVCGSGLKSVALA
AQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDG
LMCATHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTA
EIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTAGNAS
GINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQ
KALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALG
HPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER
3D structure
PDB5f38 Crystal structure of a thiolase from Escherichia coli at 1.8 angstrom resolution.
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C88 A346 A376 L378
Catalytic site (residue number reindexed from 1) C90 A348 A378 L380
Enzyme Commision number 2.3.1.9: acetyl-CoA C-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 5UG D C88 L149 A244 S248 I250 A319 F320 H349 C90 L151 A246 S250 I252 A321 F322 H351
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

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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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