› 2hv7

X-ray diffraction
2.5Å resolution

Crystal structure of phosphotyrosyl phosphatase activator bound to ATPgammaS

Released:
DOI: 10.2210/pdb2hv7/pdb
PDB entry 2hv7 coloured by chain, front view.
PDB entry 2hv7 coloured by chain, side view.
PDB entry 2hv7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and mechanism of the phosphotyrosyl phosphatase activator.
Chao Y, Xing Y, Chen Y, Xu Y, Lin Z, Li Z, Jeffrey PD, Stock JB, Shi Y
Mol Cell 23 535-46 (2006)
PMID: 16916641

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-556669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 2A activator Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 323 amino acids
Theoretical weight: 36.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15257 (Residues: 1-358; Coverage: 90%)
  • Best match: Q15257-2 (Residues: 1-323)
Gene names: PPP2R4, PTPA
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

1 bound ligand:
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 80.041Å b: 86.096Å c: 95.099Å
α: 73.91° β: 89.97° γ: 73.31°
R-values:
R R work R free
0.25 0.249 0.312
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
6 more

2 mentions without citation

Identification of candidate biomarkers and therapeutic agents for heart failure by bioinformatics analysis.
Kolur et al. (2021)
1 more