› 1o90

X-ray diffraction
3.1Å 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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase isoform type-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 43.64 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13444 (Residues: 1-397; Coverage: 100%)
Gene names: Ams1, Mat1a
Sequence domains:
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

4 bound ligands:
Ligand LIS 1 x LIS
Ligand PO4 3 x PO4
Ligand MG 3 x MG
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P4122
Unit cell:
a: 114.89Å b: 114.89Å c: 161.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.244 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

S-adenosylmethionine and its products.
Grillo et al. (2008)
4 more

2 mentions without citation

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