PDBe 2o2k

X-ray diffraction
1.6Å resolution

Crystal Structure of the Activation Domain of Human Methionine Synthase Isoform/Mutant D963E/K1071N

Released:

Function and Biology Details

Reaction catalysed:
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
Biochemical function:
  • not assigned
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: 355 amino acids
Theoretical weight: 40.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99707 (Residues: 924-1265; Coverage: 27%)
Gene name: MTR
Sequence domains: Vitamin B12 dependent methionine synthase, activation domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 77.854Å b: 90.051Å c: 123.006Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.248
Expression system: Escherichia coli BL21(DE3)