› 4h9v

X-ray diffraction
1.97Å resolution

Structure of Geobacillus kaustophilus lactonase, mutant E101G/R230C with Zn2+

Released:
DOI: 10.2210/pdb4h9v/pdb
PDB entry 4h9v coloured by chain, front view.
PDB entry 4h9v coloured by chain, side view.
PDB entry 4h9v coloured by chain, top view.
Source organism: Geobacillus kaustophilus HTA426
Primary publication:
Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase.
Xue B, Chow JY, Baldansuren A, Yap LL, Gan YH, Dikanov SA, Robinson RC, Yew WS
Biochemistry 52 2359-70 (2013)
PMID: 23461395

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-177400 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphotriesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 36.75 KDa
Source organism: Geobacillus kaustophilus HTA426
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5KZU5 (Residues: 1-326; Coverage: 100%)
Gene name: GK1506
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand FE 2 x FE
Ligand ZN 2 x ZN
Ligand OH 2 x OH
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 51.28Å b: 130.208Å c: 51.29Å
α: 90° β: 96.33° γ: 90°
R-values:
R R work R free
0.184 0.182 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Quorum quenching agents: resources for antivirulence therapy.
Tang et al. (2014)
2 more

1 mention without citation

Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase.
Xue et al. (2013)