Structure analysis

Structure of ParF-ADP form 2

X-ray diffraction
2.45Å resolution
Source organism: Escherichia coli
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9303.61 Å2
Buried surface area: 827.28 Å2
Dissociation area: 80.82 Å2
Dissociation energy (ΔGdiss): 12.65 kcal/mol
Dissociation entropy (TΔSdiss): -1.46 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-109275
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9794.34 Å2
Buried surface area: 815.05 Å2
Dissociation area: 79 Å2
Dissociation energy (ΔGdiss): 12.68 kcal/mol
Dissociation entropy (TΔSdiss): -1.46 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-109275
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 17427.39 Å2
Buried surface area: 3312.89 Å2
Dissociation area: 835.28 Å2
Dissociation energy (ΔGdiss): 5.35 kcal/mol
Dissociation entropy (TΔSdiss): 12.38 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-109276

Macromolecules

Chains: A, B
Length: 206 amino acids
Theoretical weight: 22.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: B0ZE06 (Residues: 1-206; Coverage: 100%)
Gene names: CG831_004316, DNQ45_07005, EIZ93_19540, HEP30_021835, pOLA52_52, parF
Pfam: CobQ/CobB/MinD/ParA nucleotide binding domain
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

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