Structure analysis

Protein Phosphatase, New Crystal Form

X-ray diffraction
2.38Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 16914.5 Å2
Buried surface area: 1827.3 Å2
Dissociation area: 696.27 Å2
Dissociation energy (ΔGdiss): -2.68 kcal/mol
Dissociation entropy (TΔSdiss): 12.21 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-151702
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 16835.91 Å2
Buried surface area: 1859.3 Å2
Dissociation area: 714.23 Å2
Dissociation energy (ΔGdiss): -1.82 kcal/mol
Dissociation entropy (TΔSdiss): 12.22 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-151702
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 16859.34 Å2
Buried surface area: 1821.54 Å2
Dissociation area: 689.3 Å2
Dissociation energy (ΔGdiss): -3.01 kcal/mol
Dissociation entropy (TΔSdiss): 12.21 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-151702

Macromolecules

Chains: A, B, C, D, E, F
Length: 203 amino acids
Theoretical weight: 23.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30305 (Residues: 391-580; Coverage: 33%)
Gene names: CDC25B, CDC25HU2
Pfam: Rhodanese-like domain
InterPro:
CATH: Rhodanese-like domain
SCOP: Cell cycle control phosphatase, catalytic domain

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