› 3f4d

X-ray diffraction
2.36Å resolution

Crystal structure of organophosphorus hydrolase from Geobacillus stearothermophilus strain 10

Released:
DOI: 10.2210/pdb3f4d/pdb
PDB entry 3f4d coloured by chain, front view.
PDB entry 3f4d coloured by chain, side view.
PDB entry 3f4d coloured by chain, top view.
Source organism: Geobacillus stearothermophilus 10
Primary publication:
Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.
Hawwa R, Aikens J, Turner RJ, Santarsiero BD, Mesecar AD
Arch Biochem Biophys 488 109-20 (2009)
PMID: 19615330

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112188 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Organophosphorus hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 37.28 KDa
Source organism: Geobacillus stearothermophilus 10
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VX06 (Residues: 1-326; Coverage: 98%)
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand CO 4 x CO
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 47.166Å b: 156.734Å c: 50.209Å
α: 90° β: 116.21° γ: 90°
R-values:
R R work R free
0.17 0.17 0.249
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Enzyme promiscuity: a mechanistic and evolutionary perspective.
Khersonsky et al. (2010)
6 more

6 mentions without citation

Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily.
Chow et al. (2010)
5 more