1spb

X-ray diffraction
2Å resolution

SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133531 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN' Chain: P
Molecule details ›
Chain: P
Length: 78 amino acids
Theoretical weight: 8.52 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00782 (Residues: 31-36, 37-107; Coverage: 22%)
Gene name: apr
Sequence domains: Fervidolysin N-terminal prodomain
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9
Subtilisin BPN' Chain: S
Molecule details ›
Chain: S
Length: 266 amino acids
Theoretical weight: 26.62 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 76%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21212
Unit cell:
a: 74.1Å b: 77.85Å c: 57.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 not available not available
Expression system: Escherichia coli