5dmm

X-ray diffraction
1.78Å resolution

Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated form

Released:

Function and Biology Details

Reaction catalysed:
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homocysteine S-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 33.46 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47690 (Residues: 1-310; Coverage: 100%)
Gene names: JW0253, b0261, mmuM, yagD
Sequence domains: Homocysteine S-methyltransferase
Structure domains: Homocysteine-binding-like domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: I222
Unit cell:
a: 78.949Å b: 85.924Å c: 87.662Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.205
Expression system: Escherichia coli