2yg5

X-ray diffraction
1.9Å resolution

Structure-based redesign of cofactor binding in Putrescine Oxidase: A394C mutant

Released:
Source organism: Rhodococcus erythropolis

Function and Biology Details

Reaction catalysed:
Putrescine + O(2) + H(2)O = 4-aminobutanal + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-109142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amine oxidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 49.43 KDa
Source organism: Rhodococcus erythropolis
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: B0F9F6 (Residues: 1-453; Coverage: 100%)
Gene name: puo
Sequence domains: Flavin containing amine oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P4122
Unit cell:
a: 102.003Å b: 102.003Å c: 130.361Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.242
Expression system: Escherichia coli K-12