› 3kve

X-ray diffraction
2.57Å resolution

Structure of native L-amino acid oxidase from Vipera ammodytes ammodytes: stabilization of the quaternary structure by divalent ions and structural changes in the dynamic active site

Released:
DOI: 10.2210/pdb3kve/pdb
PDB entry 3kve coloured by chain, front view.
PDB entry 3kve coloured by chain, side view.
PDB entry 3kve coloured by chain, top view.
Source organism: Vipera ammodytes ammodytes
Entry authors: Gergiova D, Murakami MT, Perbandt M, Arni RK, Betzel C

Function and Biology Details

Reaction catalysed: 
An L-amino acid + H(2)O + O(2) = a 2-oxo carboxylate + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-amino-acid oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 486 amino acids
Theoretical weight: 55.01 KDa
Source organism: Vipera ammodytes ammodytes
UniProt:
  • Canonical: P0DI84 (Residues: 1-484; Coverage: 100%)
Sequence domains: Flavin containing amine oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
2 bound ligands:
Ligand NAG 4 x NAG
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: C2
Unit cell:
a: 196.978Å b: 95.839Å c: 108.442Å
α: 90° β: 92.53° γ: 90°
R-values:
R R work R free
0.195 0.191 0.276

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