Structure analysis

Crystal structure of ATPase domain of Ssb1 chaperone, a member of the HSP70 family, from Saccharomyces cerevisiae

X-ray diffraction
1.92Å resolution
Source organism: Saccharomyces cerevisiae
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 17582.63 Å2
Buried surface area: 787.47 Å2
Dissociation area: 36.86 Å2
Dissociation energy (ΔGdiss): 5.61 kcal/mol
Dissociation entropy (TΔSdiss): -1.47 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145854
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 17100.54 Å2
Buried surface area: 901.81 Å2
Dissociation area: 152.42 Å2
Dissociation energy (ΔGdiss): 3.78 kcal/mol
Dissociation entropy (TΔSdiss): 0.86 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145854

Macromolecules

Chains: A, B
Length: 387 amino acids
Theoretical weight: 42.1 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11484 (Residues: 1-384; Coverage: 63%)
Gene names: SSB1, YDL229W, YG101
Pfam: Hsp70 protein
InterPro:
CATH:

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