› 2cye

X-ray diffraction
1.9Å resolution

Crystal structure of Thioesterase complexed with coenzyme A and Zn from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb2cye/pdb
PDB entry 2cye coloured by chain, front view.
PDB entry 2cye coloured by chain, side view.
PDB entry 2cye coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of the putative thioesterase protein TTHA1846 from Thermus thermophilus HB8 complexed with coenzyme A and a zinc ion.
Hosaka T, Murayama K, Kato-Murayama M, Urushibata A, Akasaka R, Terada T, Shirouzu M, Kuramitsu S, Yokoyama S
Acta Crystallogr. D Biol. Crystallogr. 65 767-76 (2009)
PMID: 19622860

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-177848 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 133 amino acids
Theoretical weight: 15.27 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SH84 (Residues: 1-133; Coverage: 100%)
Gene name: TTHA1846
Sequence domains: Thioesterase-like superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand COA 4 x COA
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2
Unit cell:
a: 89.53Å b: 55.817Å c: 110.147Å
α: 90° β: 102.42° γ: 90°
R-values:
R R work R free
0.208 0.208 0.242
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A strategy to enhance and modify fatty acid synthesis in Corynebacterium glutamicum and Escherichia coli: overexpression of acyl-CoA thioesterases.
Liu et al. (2023)
1 more

3 mentions without citation

Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.
Pidugu et al. (2009)
2 more