› 2a2k

X-ray diffraction
1.52Å resolution

Crystal Structure of an active site mutant, C473S, of Cdc25B Phosphatase Catalytic Domain

Released:
DOI: 10.2210/pdb2a2k/pdb
PDB entry 2a2k coloured by chain, front view.
PDB entry 2a2k coloured by chain, side view.
PDB entry 2a2k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Experimental validation of the docking orientation of Cdc25 with its Cdk2-CycA protein substrate.
Sohn J, Parks JM, Buhrman G, Brown P, Kristjánsdóttir K, Safi A, Edelsbrunner H, Yang W, Rudolph J
Biochemistry 44 16563-73 (2005)
PMID: 16342947

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
M-phase inducer phosphatase 2 Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 20.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P30305 (Residues: 391-564; Coverage: 30%)
Gene names: CDC25B, CDC25HU2
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 50.247Å b: 70.933Å c: 74.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.191
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

The molecular architecture of protein-protein binding sites.
Reichmann et al. (2007)
6 more

4 mentions without citation

Inhibition of CDC25B phosphatase through disruption of protein-protein interaction.
Lund et al. (2015)
3 more