› 6pcc

X-ray diffraction
1.96Å resolution

Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex hexanoyl coenzyme A

Released:
DOI: 10.2210/pdb6pcc/pdb
PDB entry 6pcc coloured by chain, front view.
PDB entry 6pcc coloured by chain, side view.
PDB entry 6pcc coloured by chain, top view.
Source organism: Pseudomonas putida KT2440
Primary publication:
Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
Bhaskar S, Steer DL, Anand R, Panjikar S
OpenAccess logo J Struct Biol X 4 100018 (2020)
PMID: 32647822

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183498 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoadipyl-CoA thiolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 423 amino acids
Theoretical weight: 44.45 KDa
Source organism: Pseudomonas putida KT2440
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q88N39 (Residues: 1-400; Coverage: 100%)
Gene names: PP_1377, pcaF-I
Sequence domains:

Ligands and Environments


Cofactor: Ligand COA 4 x COA
2 bound ligands:
Ligand O8Y 4 x O8Y
Ligand GOL 4 x GOL
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 111.393Å b: 116.397Å c: 127.902Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.208
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

The 3-ketoacyl-CoA thiolase: an engineered enzyme for carbon chain elongation of chemical compounds.
Liu et al. (2020)
1 other article

1 mention without citation

Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
Bhaskar et al. (2020)