› 4o98

X-ray diffraction
2.25Å resolution

Crystal structure of Pseudomonas oleovorans PoOPH mutant H250I/I263W

Released:
DOI: 10.2210/pdb4o98/pdb
PDB entry 4o98 coloured by chain, front view.
PDB entry 4o98 coloured by chain, side view.
PDB entry 4o98 coloured by chain, top view.
Source organism: Pseudomonas oleovorans
Primary publication:
Switching a newly discovered lactonase into an efficient and thermostable phosphotriesterase by simple double mutations His250Ile/Ile263Trp.
Luo XJ, Kong XD, Zhao J, Chen Q, Zhou J, Xu JH
Biotechnol Bioeng 111 1920-30 (2014)
PMID: 24771278

Function and Biology Details

Biochemical function:
  • not assigned
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-100908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 36.54 KDa
Source organism: Pseudomonas oleovorans
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0B4J186 (Residues: 1-337; Coverage: 100%)
Gene name: OPHC
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P61
Unit cell:
a: 116.742Å b: 116.742Å c: 83.395Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.177 0.22
Expression system: Escherichia coli

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Citations

6 review citations

Quorum quenching: role in nature and applied developments.
Grandclément et al. (2016)
5 more