3sws

X-ray diffraction
1.86Å resolution

Crystal Structure of the Quinone Form of Methylamine Dehydrogenase in Complex with the Diferric Form of MauG

Released:
Entry authors: Jensen LMR, Wilmot CM

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Methylamine utilization protein MauG Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 41.15 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Paracoccus denitrificans PD1222
UniProt:
  • Canonical: Q51658 (Residues: 21-387; Coverage: 100%)
Gene names: Pden_4736, mauG
Sequence domains: Di-haem cytochrome c peroxidase
Structure domains: Cytochrome c-like domain
Methylamine dehydrogenase (amicyanin) Chains: C, E
Molecule details ›
Chains: C, E
Length: 137 amino acids
Theoretical weight: 15.04 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Rhodobacter sphaeroides
UniProt:
  • Canonical: A1BBA0 (Residues: 58-188; Coverage: 70%)
Gene name: Pden_4733
Sequence domains: Methylamine dehydrogenase, L chain
Structure domains: Methylamine/Aralkylamine dehydrogenase light chain
Methylamine dehydrogenase heavy chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 386 amino acids
Theoretical weight: 42.45 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Rhodobacter sphaeroides
UniProt:
  • Canonical: A1BB97 (Residues: 32-417; Coverage: 99%)
Gene name: Pden_4730
Sequence domains: Methylamine dehydrogenase heavy chain (MADH)
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 55.222Å b: 99.422Å c: 102.832Å
α: 64.77° β: 74.77° γ: 75.14°
R-values:
R R work R free
0.138 0.136 0.178
Expression systems:
  • Paracoccus denitrificans PD1222
  • Rhodobacter sphaeroides