› 1st3

X-ray diffraction
1.4Å resolution

THE CRYSTAL STRUCTURE OF THE BACILLUS LENTUS ALKALINE PROTEASE, SUBTILISIN BL, AT 1.4 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1st3/pdb
PDB entry 1st3 coloured by chain, front view.
PDB entry 1st3 coloured by chain, side view.
PDB entry 1st3 coloured by chain, top view.
Source organism: Lederbergia lenta
Primary publication:
The crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4 A resolution.
Goddette DW, Paech C, Yang SS, Mielenz JR, Bystroff C, Wilke ME, Fletterick RJ
J Mol Biol 228 580-95 (1992)
PMID: 1453465

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin BL Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 26.83 KDa
Source organism: Lederbergia lenta
Expression system: Not provided
UniProt:
  • Canonical: P29599 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 53.093Å b: 61.49Å c: 75.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

19 citation in other articles

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

6 mentions without citation

Olefin metathesis for chemical biology.
Binder et al. (2008)
5 more