› 1be8

X-ray diffraction
2.2Å resolution

TRANS-CINNAMOYL-SUBTILISIN IN WATER

Released:
DOI: 10.2210/pdb1be8/pdb
PDB entry 1be8 coloured by chain, front view.
PDB entry 1be8 coloured by chain, side view.
PDB entry 1be8 coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water.
Schmitke JL, Stern LJ, Klibanov AM
Proc Natl Acad Sci U S A 95 12918-23 (1998)
PMID: 9789015

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 licheniformis
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

2 bound ligands:
Ligand CA 1 x CA
Ligand TCA 1 x TCA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 76.965Å b: 55.039Å c: 53.643Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.223

Quick links

Citations

3 review citations

Protein flexibility in docking and surface mapping.
Lexa et al. (2012)
2 more

3 mentions without citation

Multiple structural alignment by secondary structures: algorithm and applications.
Dror et al. (2003)
2 more