› 4gah

X-ray diffraction
2.3Å resolution

Human acyl-CoA thioesterases 4 in complex with undecan-2-one-CoA inhibitor

Released:
DOI: 10.2210/pdb4gah/pdb
PDB entry 4gah coloured by chain, front view.
PDB entry 4gah coloured by chain, side view.
PDB entry 4gah coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Correlation of structure and function in the human hotdog-fold enzyme hTHEM4.
Zhao H, Lim K, Choudry A, Latham JA, Pathak MC, Dominguez D, Luo L, Herzberg O, Dunaway-Mariano D
Biochemistry 51 6490-2 (2012)
PMID: 22871024

Function and Biology Details

Reaction catalysed: 
Palmitoyl-CoA + H(2)O = CoA + palmitate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A thioesterase THEM4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5T1C6 (Residues: 40-240; Coverage: 84%)
Gene names: CTMP, THEM4
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments


Cofactor: Ligand 0ET 3 x 0ET
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 56.608Å b: 58.777Å c: 135.436Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.257
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enzyme promiscuity: engine of evolutionary innovation.
Pandya et al. (2014)
4 other articles

6 mentions without citation

Using parallelized incremental meta-docking can solve the conformational sampling issue when docking large ligands to proteins.
Devaurs et al. (2019)
5 more