› 1sbc

X-ray diffraction
2.5Å resolution

THE REFINED CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG AT 2.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1sbc/pdb
PDB entry 1sbc coloured by chain, front view.
PDB entry 1sbc coloured by chain, side view.
PDB entry 1sbc coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution.
Neidhart DJ, Petsko GA
Protein Eng 2 271-6 (1988)
PMID: 3150541

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-133525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Carlsberg Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene names: apr, subC
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 76.67Å b: 55.65Å c: 53.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 not available not available
Expression system: Not provided

Quick links

Citations

45 citation in other articles

Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins.
Mulder et al. (1999)
44 more

13 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
12 more