› 3sxt

X-ray diffraction
1.81Å resolution

Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG

Released:
DOI: 10.2210/pdb3sxt/pdb
PDB entry 3sxt coloured by chain, front view.
PDB entry 3sxt coloured by chain, side view.
PDB entry 3sxt coloured by chain, top view.
Source organism: Paracoccus denitrificans PD1222
Entry authors: Jensen LMR, Wilmot CM

Function and Biology Details

Reaction catalysed: 
Methylamine + H(2)O + 2 oxidized [amicyanin] = formaldehyde + NH(3) + 2 reduced [amicyanin]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-106574 (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: Cereibacter 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: Cereibacter 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


Cofactor: Ligand HEC 4 x HEC
3 bound ligands:
Ligand CA 2 x CA
Ligand NA 4 x NA
Ligand EDO 5 x EDO
1 modified residue:
Ligand TOQ 2 x TOQ

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 62.639Å b: 135.664Å c: 111.557Å
α: 90° β: 97.37° γ: 90°
R-values:
R R work R free
0.147 0.145 0.187
Expression systems:
  • Paracoccus denitrificans PD1222
  • Cereibacter sphaeroides

Quick links