Structure of PDB 1qfl Chain D

Receptor sequence

>1qflD (length=389) Species: 350 (Zoogloea ramigera)

SIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVI
LGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQI
ATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFY
GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI
VKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGA
AAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA
GWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGAS
GARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL

3D structure

• PDB: 1qfl A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.
• Chain: D
• Resolution: 1.92 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C89 H348 C378 G380
• Catalytic site (residue number reindexed from 1): C86 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	D	C89 H156 M157 R220 L231 F235 A243 S247 L249 F319 H348	C86 H153 M154 R217 L228 F232 A240 S244 L246 F316 H345

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:1qfl, PDBe:1qfl, PDBj:1qfl
• PDBsum: 1qfl
• PubMed: 10545327
• UniProt: P07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)