Structure of PDB 4o9c Chain C

Receptor sequence

>4o9cC (length=393) Species: 381666 (Cupriavidus necator H16)

MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSE
VIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVSGSGLKAVMLAAN
AIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWD
VYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV
PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGL
NDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRA
LSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGHP
IGASGCRILVTLLHEMKRRDAKKGLASLCIGGGMGVALAVERK

3D structure

• PDB: 4o9c Crystal structure and biochemical characterization of PhaA from Ralstonia eutropha, a polyhydroxyalkanoate-producing bacterium.
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S88 H349 C379 G381
• Catalytic site (residue number reindexed from 1): S88 H349 C379 G381
• 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	S88 L148 R221 F236 A244 S248 L250 A319 F320 H349	S88 L148 R221 F236 A244 S248 L250 A319 F320 H349

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:4o9c, PDBe:4o9c, PDBj:4o9c
• PDBsum: 4o9c
• PubMed: 25152395
• UniProt: P14611|THIL_CUPNH Acetyl-CoA acetyltransferase (Gene Name=phaA)