Structure analysis

Crystal Structure of the First Nucelotide Binding Domain of ClpB

X-ray diffraction
1.8Å 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: 10100 Å2
Buried surface area: 100 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 9 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -8 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 195 amino acids
Theoretical weight: 21.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63284 (Residues: 159-351; Coverage: 23%)
Gene names: JW2573, b2592, clpB, htpM
Pfam: ATPase family associated with various cellular activities (AAA)
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases
SCOP: Extended AAA-ATPase domain

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