› 4kfe

X-ray diffraction
2.1Å resolution

Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 7.0

Released:
DOI: 10.2210/pdb4kfe/pdb
PDB entry 4kfe coloured by chain, front view.
PDB entry 4kfe coloured by chain, side view.
PDB entry 4kfe coloured by chain, top view.
Source organism: Ogataea angusta
Primary publication:
Structural evidence for the semiquinone in a copper amine oxidase from Hansenula polymorpha: implications for the catalytic mechanism
Johnson BJ, Yukl ET, Klema VJ, Klinman JP, Wilmot CM
J. Biol. Chem. (2013)

Function and Biology Details

Reaction catalysed: 
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal primary amine oxidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 692 amino acids
Theoretical weight: 77.66 KDa
Source organism: Ogataea angusta
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P12807 (Residues: 1-692; Coverage: 100%)
Gene name: AMO
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand CU 6 x CU
Ligand PEO 6 x PEO
Ligand FOR 3 x FOR
Ligand GOL 52 x GOL
Ligand PO4 3 x PO4
1 modified residue:
Ligand TYY 6 x TYY

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 103.577Å b: 222.836Å c: 103.619Å
α: 90° β: 95.87° γ: 90°
R-values:
R R work R free
0.132 0.129 0.18
Expression system: Saccharomyces cerevisiae

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