3k13

X-ray diffraction
2Å resolution

Structure of the pterin-binding domain MeTr of 5-methyltetrahydrofolate-homocysteine methyltransferase from Bacteroides thetaiotaomicron

Released:
Source organism: Bacteroides thetaiotaomicron
Entry authors: Cuff ME, Li H, Cobb G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183811 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 300 amino acids
Theoretical weight: 33.65 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8ABD0 (Residues: 345-641; Coverage: 33%)
Gene name: BT_0180
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments


Cofactor: Ligand THH 3 x THH
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 137.652Å b: 79.992Å c: 127.068Å
α: 90° β: 90.12° γ: 90°
R-values:
R R work R free
0.162 0.16 0.188
Expression system: Escherichia coli BL21