› 1fug

X-ray diffraction
3.2Å resolution

S-ADENOSYLMETHIONINE SYNTHETASE

Released:
DOI: 10.2210/pdb1fug/pdb
PDB entry 1fug coloured by chain, front view.
PDB entry 1fug coloured by chain, side view.
PDB entry 1fug coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification.
Fu Z, Hu Y, Markham GD, Takusagawa F
J Biomol Struct Dyn 13 727-39 (1996)
PMID: 8723769

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-141653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 41.87 KDa
Source organism: Escherichia coli
Expression system: Not provided
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 121Å b: 121Å c: 171Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.29
Expression system: Not provided

Quick links

Citations

1 review citation

S-Adenosylmethionine: a control switch that regulates liver function.
Mato et al. (2002)
17 other articles

11 mentions without citation

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