› 2w8s

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF A catalytically promiscuous PHOSPHONATE MONOESTER HYDROLASE FROM Burkholderia caryophylli

Released:
DOI: 10.2210/pdb2w8s/pdb
PDB entry 2w8s coloured by chain, front view.
PDB entry 2w8s coloured by chain, side view.
PDB entry 2w8s coloured by chain, top view.
Source organism: Trinickia caryophylli
Primary publication:
An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.
van Loo B, Jonas S, Babtie AC, Benjdia A, Berteau O, Hyvönen M, Hollfelder F
Proc Natl Acad Sci U S A 107 2740-5 (2010)
PMID: 20133613

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional alkaline phosphatase superfamily protein PehA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 543 amino acids
Theoretical weight: 61.22 KDa
Source organism: Trinickia caryophylli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q45087 (Residues: 1-514; Coverage: 100%)
Gene name: pehA
Sequence domains: Sulfatase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 4 x ZN
Ligand FE 4 x FE
Ligand SO4 7 x SO4
Ligand GOL 4 x GOL
1 modified residue:
Ligand FGL 4 x FGL

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 57.7Å b: 200.1Å c: 211.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

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

6 mentions without citation

High resolution crystal structure of the catalytic domain of MCR-1.
Ma et al. (2016)
5 more