› 1sub

X-ray diffraction
1.75Å resolution

CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN

Released:
DOI: 10.2210/pdb1sub/pdb
PDB entry 1sub coloured by chain, front view.
PDB entry 1sub coloured by chain, side view.
PDB entry 1sub coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Calcium-independent subtilisin by design.
Gallagher T, Bryan P, Gilliland GL
Proteins 16 205-13 (1993)
PMID: 8332608

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: 27.57 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand K 1 x K
Ligand ACN 1 x ACN
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 41.77Å b: 79.52Å c: 37.22Å
α: 90° β: 114.97° γ: 90°
R-values:
R R work R free
0.148 not available not available
Expression system: Not provided

Quick links

Citations

1 review citation

Protein engineering of subtilisin.
Bryan PN. (2000)
20 other articles

2 mentions without citation

Multiple structural alignment by secondary structures: algorithm and applications.
Dror et al. (2003)
1 more