› 2wd9

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF HUMAN ACYL-COA SYNTHETASE MEDIUM-CHAIN FAMILY MEMBER 2A (L64P MUTATION) IN COMPLEX WITH IBUPROFEN

Released:
DOI: 10.2210/pdb2wd9/pdb
PDB entry 2wd9 coloured by chain, front view.
PDB entry 2wd9 coloured by chain, side view.
PDB entry 2wd9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.
Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW
J Mol Biol 388 997-1008 (2009)
PMID: 19345228

Function and Biology Details

Reactions catalysed: 
ATP + a medium-chain fatty acid + CoA = AMP + diphosphate + a medium-chain acyl-CoA
ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A synthetase ACSM2A, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 569 amino acids
Theoretical weight: 63.21 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q08AH3 (Residues: 15-576; Coverage: 97%)
Gene names: ACSM2, ACSM2A, MACS2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand IBP 3 x IBP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 98.32Å b: 98.32Å c: 381.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.235 0.255
Expression system: Trichoplusia ni

Quick links

Citations

7 review citations

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
6 more

2 mentions without citation

The Recognition of Identical Ligands by Unrelated Proteins.
Barelier et al. (2015)
1 more