› 1mxa

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase Chain: A
Molecule details ›
Chain: A
Length: 383 amino acids
Theoretical weight: 41.87 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A817 (Residues: 2-384; Coverage: 100%)
Gene names: JW2909, b2942, metK, metX
Sequence domains:
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

4 bound ligands:
Ligand PO4 1 x PO4
Ligand MG 2 x MG
Ligand K 2 x K
Ligand POP 1 x POP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6222
Unit cell:
a: 128.9Å b: 128.9Å c: 139.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.257

Quick links

Citations

9 review citations

Metabolism of sulfur amino acids in Saccharomyces cerevisiae.
Thomas et al. (1997)
8 more

4 mentions without citation

Structure-function relationships in methionine adenosyltransferases.
Markham et al. (2009)
3 more