PDBe 1bmt

X-ray diffraction
3Å resolution

HOW A PROTEIN BINDS B12: A 3.O ANGSTROM X-RAY STRUCTURE OF THE B12-BINDING DOMAINS OF METHIONINE SYNTHASE

Released:

Function and Biology Details

Reaction catalysed:
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 27.21 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P13009 (Residues: 651-896; Coverage: 20%)
Gene names: JW3979, b4019, metH
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 96.7Å b: 55.3Å c: 103.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Not provided