› 1rku

X-ray diffraction
1.47Å resolution

Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa

Released:
DOI: 10.2210/pdb1rku/pdb
PDB entry 1rku coloured by chain, front view.
PDB entry 1rku coloured by chain, side view.
PDB entry 1rku coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity.
Singh SK, Yang K, Karthikeyan S, Huynh T, Zhang X, Phillips MA, Zhang H
J Biol Chem 279 13166-73 (2004)
PMID: 14699121

Function and Biology Details

Reaction catalysed: 
O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoserine phosphatase ThrH Chains: A, B
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 23.68 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9I2Y2 (Residues: 1-205; Coverage: 100%)
Gene names: PA1757, thrH
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: C2221
Unit cell:
a: 71.749Å b: 97.236Å c: 131.772Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 citation in other articles

Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes.
Burroughs et al. (2006)
12 more

1 mention without citation

Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases.
London et al. (2015)