3sby

X-ray diffraction
2.71Å resolution

Crystal Structure of SeMet-Substituted Apo-MMACHC (1-244), a human B12 processing enzyme

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
2 cob(II)alamin-[cyanocobalamin reductase] + 2 hydrogen cyanide + NADP(+) = 2 cyanocob(III)alamin + 2 [cyanocobalamin reductase] + NADPH
An alkylcobalamin + [alkylcobalamin reductase] + glutathione = cob(I)alamin-[alkylcobalamin reductase] + an S-alkylglutathione
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-195250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyanocobalamin reductase / alkylcobalamin dealkylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 29.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4U1 (Residues: 1-244; Coverage: 87%)
Gene name: MMACHC
Sequence domains: Methylmalonic aciduria and homocystinuria type C family

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P65
Unit cell:
a: 69.267Å b: 69.267Å c: 201.848Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.276 0.228 0.29
Expression system: Escherichia coli