› 4ien

X-ray diffraction
2Å resolution

Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18

Released:
DOI: 10.2210/pdb4ien/pdb
PDB entry 4ien coloured by chain, front view.
PDB entry 4ien coloured by chain, side view.
PDB entry 4ien coloured by chain, top view.
Source organism: Neisseria meningitidis FAM18
Primary publication:
Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.
Khandokar YB, Londhe A, Patil S, Forwood JK
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 1303-6 (2013)
PMID: 24192375

Function and Biology Details

Reaction catalysed: 
Acyl-CoA + H(2)O = CoA + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HotDog ACOT-type domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 163 amino acids
Theoretical weight: 18.28 KDa
Source organism: Neisseria meningitidis FAM18
Expression system: Escherichia coli
UniProt:
  • Canonical: A1KUS8 (Residues: 1-160; Coverage: 100%)
Gene name: NMC1417
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments


Cofactor: Ligand COA 4 x COA
2 bound ligands:
Ligand GDP 4 x GDP
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P213
Unit cell:
a: 152.52Å b: 152.52Å c: 152.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.194
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency.
Tsimbalyuk et al. (2020)
1 more

2 mentions without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)
1 more