1mae

X-ray diffraction
2.8Å resolution

The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methylamine dehydrogenase light chain Chain: L
Molecule details ›
Chain: L
Length: 124 amino acids
Theoretical weight: 13.65 KDa
Source organism: Paracoccus versutus
Expression system: Not provided
UniProt:
  • Canonical: P22641 (Residues: 64-187; Coverage: 95%)
Gene names: madB, mauA
Sequence domains: Methylamine dehydrogenase, L chain
Structure domains: Methylamine/Aralkylamine dehydrogenase light chain
Methylamine dehydrogenase heavy chain Chain: H
Molecule details ›
Chain: H
Length: 373 amino acids
Theoretical weight: 38.03 KDa
Source organism: Paracoccus versutus
Expression system: Not provided
UniProt:
  • Canonical: P23006 (Residues: 58-423; Coverage: 93%)
Gene names: madA, mauB
Sequence domains: Methylamine dehydrogenase heavy chain (MADH)

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 129.784Å b: 129.784Å c: 104.334Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 not available not available
Expression system: Not provided