4ccz

X-ray diffraction
2.7Å resolution

Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains

Released:
Source organism: Homo sapiens
Entry authors: Vollmar M, Kiyani W, Krojer T, Goubin S, Burgess-Brown N, von Delft F, Oppermann U, Edwards A, Arrowsmith C, Bountra C, Yue WW

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chain: A
Molecule details ›
Chain: A
Length: 644 amino acids
Theoretical weight: 70.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99707 (Residues: 16-657; Coverage: 51%)
Gene name: MTR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand THG 1 x THG
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: I23
Unit cell:
a: 166.803Å b: 166.803Å c: 166.803Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.274
Expression system: Escherichia coli BL21(DE3)