Structure analysis

High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)

X-ray diffraction
1.38Å resolution
Source organism: Bacillus subtilis
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 25000 Å2
Buried surface area: 1800 Å2
Dissociation area: 650 Å2
Dissociation energy (ΔGdiss): 5 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -65 kcal/mol
Symmetry number: 1

Macromolecules

Chains: 1, 2
Length: 357 amino acids
Theoretical weight: 36.32 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RR56 (Residues: 189-545; Coverage: 65%)
Gene name: kscp
Pfam: Subtilase family
InterPro:
CATH: Rossmann fold
SCOP: Serine-carboxyl proteinase, SCP

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