Structure of PDB 2vtz Chain C

Receptor sequence

>2vtzC (length=389) Species: 350 (Zoogloea ramigera)

SIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVI
LGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLAGSGLRAVALGMQQI
ATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFY
GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI
VKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGA
AAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA
GWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGAS
GARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL

3D structure

• PDB: 2vtz 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.
• Chain: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A89 H348 C378 G380
• Catalytic site (residue number reindexed from 1): A86 H345 C375 G377
• 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	COA	C	L148 H156 R220 A243 G244 S247 G248 L249 A318 F319 H348	L145 H153 R217 A240 G241 S244 G245 L246 A315 F316 H345	MOAD: Kd=307uM

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:2vtz, PDBe:2vtz, PDBj:2vtz
• PDBsum: 2vtz
• PubMed: 19016856
• UniProt: P07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)