Structure analysis

CRYSTAL STRUCTURE OF PHYTATE COMPLEX ESCHERICHIA COLI PHYTASE AT PH 5.0. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE

X-ray diffraction
2.05Å resolution
Source organism: Escherichia coli
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 17002.02 Å2
Buried surface area: 1352.95 Å2
Dissociation area: 64.16 Å2
Dissociation energy (ΔGdiss): 15.98 kcal/mol
Dissociation entropy (TΔSdiss): 1.8 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-139374

Macromolecules

Chain: A
Length: 410 amino acids
Theoretical weight: 44.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P07102 (Residues: 23-432; Coverage: 100%)
Gene names: JW0963, appA, b0980
Pfam: Histidine phosphatase superfamily (branch 2)
InterPro:
CATH: Phosphoglycerate mutase-like
SCOP: Histidine acid phosphatase

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