› 1sbi

X-ray diffraction
2.2Å resolution

SUBTILISIN BPN' 8397 (E.C. 3.4.21.14) MUTANT (M50F, N76D, G169A, Q206C, N218S)

Released:
DOI: 10.2210/pdb1sbi/pdb
PDB entry 1sbi coloured by chain, front view.
PDB entry 1sbi coloured by chain, side view.
PDB entry 1sbi coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
A weak calcium binding site in subtilisin BPN' has a dramatic effect on protein stability.
Kidd RD, Yennawar HP, Sears P, Wong CH, Farber GK
J. Am. Chem. Soc. 118 1645-1650 (1996)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin BPN' Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 27.55 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 41.51Å b: 79.34Å c: 37.24Å
α: 90° β: 114.32° γ: 90°
R-values:
R R work R free
0.164 0.164 0.163
Expression system: Bacillus subtilis

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