Structure analysis

REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS

X-ray diffraction
2Å resolution
Source organism: Escherichia coli
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: 27932.4 Å2
Buried surface area: 8707.33 Å2
Dissociation area: 3,824.11 Å2
Dissociation energy (ΔGdiss): 38.28 kcal/mol
Dissociation entropy (TΔSdiss): 14.97 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-132772

Macromolecules

Chains: A, B
Length: 449 amino acids
Theoretical weight: 47.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 23-471; Coverage: 100%)
Gene names: JW0374, b0383, phoA
Pfam: Alkaline phosphatase
InterPro:
CATH: Alkaline Phosphatase, subunit A
SCOP: Alkaline phosphatase

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