PDBe 1g72

X-ray diffraction
1.9Å resolution

CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methanol dehydrogenase [cytochrome c] subunit 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 573 amino acids
Theoretical weight: 62.7 KDa
Source organism: Methylophilus methylotrophus W3A1
UniProt:
  • Canonical: P38539 (Residues: 1-573; Coverage: 100%)
Sequence domains: PQQ-like domain
Structure domains: Methanol Dehydrogenase; Chain A
Methanol dehydrogenase [cytochrome c] subunit 2 Chains: B, D
Molecule details ›
Chains: B, D
Length: 69 amino acids
Theoretical weight: 7.77 KDa
Source organism: Methylophilus methylotrophus W3A1
UniProt:
  • Canonical: P38540 (Residues: 23-91; Coverage: 100%)
Gene name: moxI
Structure domains: Methanol Dehydrogenase, chain B

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P21
Unit cell:
a: 98.115Å b: 69.744Å c: 109.838Å
α: 90° β: 110.29° γ: 90°
R-values:
R R work R free
0.16 0.16 0.19