› 1scn

X-ray diffraction
1.9Å resolution

INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE

Released:
DOI: 10.2210/pdb1scn/pdb
PDB entry 1scn coloured by chain, front view.
PDB entry 1scn coloured by chain, side view.
PDB entry 1scn coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative.
Steinmetz AC, Demuth HU, Ringe D
Biochemistry 33 10535-44 (1994)
PMID: 8068694

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: E
Molecule details ›
Chain: E
Length: 276 amino acids
Theoretical weight: 27.47 KDa
Source organism: Bacillus licheniformis
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

3 bound ligands:
Ligand 0EF 1 x 0EF
Ligand CA 2 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 76.5Å b: 55.4Å c: 53.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 not available not available
Expression system: Not provided

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Citations

1 review citation

Conformational homogeneity in molecular recognition by proteolytic enzymes.
Tyndall et al. (1999)
3 other articles

7 mentions without citation

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
6 more