› 1l7m

X-ray diffraction
1.48Å resolution

HIGH RESOLUTION LIGANDED STRUCTURE OF PHOSPHOSERINE PHOSPHATASE (PI COMPLEX)

Released:
DOI: 10.2210/pdb1l7m/pdb
PDB entry 1l7m coloured by chain, front view.
PDB entry 1l7m coloured by chain, side view.
PDB entry 1l7m coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states.
Wang W, Cho HS, Kim R, Jancarik J, Yokota H, Nguyen HH, Grigoriev IV, Wemmer DE, Kim SH
J Mol Biol 319 421-31 (2002)
PMID: 12051918

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoserine phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 23.78 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58989 (Residues: 1-211; Coverage: 100%)
Gene name: MJ1594
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21212
Unit cell:
a: 69.073Å b: 70.27Å c: 90.924Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.232
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Structural basis of ion pumping by Ca2+-ATPase of the sarcoplasmic reticulum.
Toyoshima et al. (2004)
13 more

6 mentions without citation

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
5 more