› 1lo9

X-ray diffraction
2.8Å resolution

X-ray crystal structure of 4-hydroxybenzoyl CoA thioesterase mutant D17N complexed with 4-hydroxybenzoyl CoA

Released:
DOI: 10.2210/pdb1lo9/pdb
PDB entry 1lo9 coloured by chain, front view.
PDB entry 1lo9 coloured by chain, side view.
PDB entry 1lo9 coloured by chain, top view.
Source organism: Pseudomonas sp. CBS3
Primary publication:
X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase.
Thoden JB, Holden HM, Zhuang Z, Dunaway-Mariano D
J Biol Chem 277 27468-76 (2002)
PMID: 11997398

Function and Biology Details

Reaction catalysed: 
4-hydroxybenzoyl-CoA + H(2)O = 4-hydroxybenzoate + CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxybenzoyl-CoA thioesterase Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 16.14 KDa
Source organism: Pseudomonas sp. CBS3
Expression system: Escherichia coli
UniProt:
  • Canonical: P56653 (Residues: 1-141; Coverage: 100%)
Sequence domains: Thioesterase-like superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments


Cofactor: Ligand BCA 1 x BCA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 52.5Å b: 55.8Å c: 93.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.147 0.247
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Enzyme promiscuity: engine of evolutionary innovation.
Pandya et al. (2014)
1 more

8 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
7 more