› 3b7w

X-ray diffraction
2Å resolution

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation

Released:
DOI: 10.2210/pdb3b7w/pdb
PDB entry 3b7w coloured by chain, front view.
PDB entry 3b7w coloured by chain, side view.
PDB entry 3b7w 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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A synthetase ACSM2A, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 570 amino acids
Theoretical weight: 63.33 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q08AH3 (Residues: 32-577; Coverage: 95%)
Gene names: ACSM2, ACSM2A, MACS2
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand CL 4 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: I222
Unit cell:
a: 98.426Å b: 109.173Å c: 176.926Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.214
Expression system: Trichoplusia ni

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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

1 mention without citation

Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase.
Reger et al. (2008)