› 1l8l

X-ray diffraction
2.51Å resolution

Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase

Released:
DOI: 10.2210/pdb1l8l/pdb
PDB entry 1l8l coloured by chain, front view.
PDB entry 1l8l coloured by chain, side view.
PDB entry 1l8l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase.
Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY
J Biol Chem 277 46651-8 (2002)
PMID: 12213811

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-160245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoserine phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P78330 (Residues: 1-225; Coverage: 100%)
Gene name: PSPH
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand APO 2 x APO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: I4
Unit cell:
a: 106.213Å b: 106.213Å c: 87.812Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.213 0.284
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Human HAD phosphatases: structure, mechanism, and roles in health and disease.
Seifried et al. (2013)
2 more

3 mentions without citation

Structural genomics of protein phosphatases.
Almo et al. (2007)
2 more