› 1ry2

X-ray diffraction
2.3Å resolution

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

Released:
DOI: 10.2210/pdb1ry2/pdb
PDB entry 1ry2 coloured by chain, front view.
PDB entry 1ry2 coloured by chain, side view.
PDB entry 1ry2 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP.
Jogl G, Tong L
Biochemistry 43 1425-31 (2004)
PMID: 14769018

Function and Biology Details

Reaction catalysed: 
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-coenzyme A synthetase 1 Chain: A
Molecule details ›
Chain: A
Length: 663 amino acids
Theoretical weight: 73.6 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01574 (Residues: 72-713; Coverage: 90%)
Gene names: ACS1, FUN44, YAL054C
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AMP 1 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3
Unit cell:
a: 107.13Å b: 107.13Å c: 54.79Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.199 0.258
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Adenylate-forming enzymes.
Schmelz et al. (2009)
5 more

8 mentions without citation

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