› 1gci

X-ray diffraction
0.78Å resolution

THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN

Released:
DOI: 10.2210/pdb1gci/pdb
PDB entry 1gci coloured by chain, front view.
PDB entry 1gci coloured by chain, side view.
PDB entry 1gci coloured by chain, top view.
Source organism: Lederbergia lenta
Primary publication:
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin.
Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R
Biochemistry 37 13446-52 (1998)
PMID: 9753430

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-151551 (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: Lederbergia lenta
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand CA 2 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 52.65Å b: 61.25Å c: 74.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.101 not available 0.103
Expression system: Bacillus subtilis

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Citations

12 review citations

Challenges in enzyme mechanism and energetics.
Kraut et al. (2003)
11 more

30 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
29 more