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KINETICS AND CRYSTAL STRUCTURE OF A MUTANT E. COLI ALKALINE PHOSPHATASE (ASP-369-->ASN): A MECHANISM INVOLVING ONE ZINC PER ACTIVE SITE

X-ray diffraction
2.5Å resolution
PDB entry 1alh coloured by chain, front view.
PDB entry 1alh coloured by chain, side view.
PDB entry 1alh coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Alkaline phosphatase
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Multimeric state: homo dimer
Accessible surface area: 26383.63 Å2
Buried surface area: 8593.7 Å2
Dissociation area: 3,791.47 Å2
Dissociation energy (ΔGdiss): 34.7 kcal/mol
Dissociation entropy (TΔSdiss): 14.96 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-132772

Macromolecules

Alkaline phosphatase
Chains: A, B
Length: 446 amino acids
Theoretical weight: 46.77 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 26-471; Coverage: 99%)
Gene names: JW0374, b0383, phoA
Pfam: Alkaline phosphatase
InterPro:
CATH: Alkaline Phosphatase, subunit A
SCOP: Alkaline phosphatase
Alkaline phosphatase in PDB entry 1alh, assembly 1, front view.
Alkaline phosphatase in PDB entry 1alh, assembly 1, side view.
Alkaline phosphatase in PDB entry 1alh, assembly 1, top view.
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