› 1xrb

X-ray diffraction
3Å resolution

S-adenosylmethionine synthetase (MAT, ATP: L-methionine S-adenosyltransferase, E.C.2.5.1.6) in which MET residues are replaced with selenomethionine residues (MSE)

Released:
DOI: 10.2210/pdb1xrb/pdb
PDB entry 1xrb coloured by chain, front view.
PDB entry 1xrb coloured by chain, side view.
PDB entry 1xrb coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of S-adenosylmethionine synthetase.
Takusagawa F, Kamitori S, Misaki S, Markham GD
J Biol Chem 271 136-47 (1996)
PMID: 8550549

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: 42.29 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

3 bound ligands:
Ligand PO4 2 x PO4
Ligand MG 2 x MG
Ligand K 2 x K
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
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
0.188 0.188 0.265

Quick links

Citations

7 review citations

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

1 mention without citation

Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE.
Xia et al. (2007)