Structure of PDB 1ou6 Chain B

Receptor sequence

>1ou6B (length=392) Species: 350 (Zoogloea ramigera)

STPSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVN
EVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGM
QQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTD
AFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIV
PFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLN
DGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKAL
ERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPI
GASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL

3D structure

• PDB: 1ou6 The surprising binding mode of a coenzyme A analogue, O-pantetheine-11-pivalate, in the catalytic cavity of bacterial biosynthetic thiolase
• Chain: B
• Resolution: 2.07 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C89 H348 C378 G380
• Catalytic site (residue number reindexed from 1): C89 H348 C378 G380
• 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	168	B	I144 L148 H156 M157 A243 S247 F319 H348	I144 L148 H156 M157 A243 S247 F319 H348

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

External links

• PDB: RCSB:1ou6, PDBe:1ou6, PDBj:1ou6
• PDBsum: 1ou6
• UniProt: P07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)