› 2yg4

X-ray diffraction
2.3Å resolution

Structure-based redesign of cofactor binding in Putrescine Oxidase: wild type bound to Putrescine

Released:
DOI: 10.2210/pdb2yg4/pdb
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PDB entry 2yg4 coloured by chain, front view.
PDB entry 2yg4 coloured by chain, side view.
PDB entry 2yg4 coloured by chain, top view.
Source organism: Rhodococcus erythropolis
Primary publication:
Structure-based redesign of cofactor binding in putrescine oxidase.
Kopacz MM, Rovida S, van Duijn E, Fraaije MW, Mattevi A
Biochemistry 50 4209-17 (2011)
PMID: 21486042

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amine oxidase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 453 amino acids
Theoretical weight: 49.4 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 2 x FAD
3 bound ligands:
Ligand 4HA 2 x 4HA
Ligand GOL 4 x GOL
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 198.59Å b: 80.61Å c: 92.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.197
Expression system: Escherichia coli K-12

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Citations

7 citation in other articles

Functional identification of two novel genes from Pseudomonas sp. strain HZN6 involved in the catabolism of nicotine.
Qiu et al. (2012)
6 more

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