1jea

X-ray diffraction
2Å resolution

ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN

Released:
Source organism: Bacillus lentus
Primary publication:
Engineered Bacillus lentus subtilisins having altered flexibility.
J. Mol. Biol. 292 97-109 (1999)
PMID: 10493860

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Savinase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 26.72 KDa
Source organism: Bacillus lentus
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: null%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 53.4Å b: 61.35Å c: 75.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 not available not available
Expression system: Bacillus subtilis