› 5jss

X-ray diffraction
1.19Å resolution

Thermolysin in complex with JC149.

Released:
DOI: 10.2210/pdb5jss/pdb
PDB entry 5jss coloured by chain, front view.
PDB entry 5jss coloured by chain, side view.
PDB entry 5jss coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Rational Design of Thermodynamic and Kinetic Binding Profiles by Optimizing Surface Water Networks Coating Protein-Bound Ligands.
Krimmer SG, Cramer J, Betz M, Fridh V, Karlsson R, Heine A, Klebe G
J Med Chem 59 10530-10548 (2016)
PMID: 27933956

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chain: E
Molecule details ›
Chain: E
Length: 316 amino acids
Theoretical weight: 34.36 KDa
Source organism: Bacillus thermoproteolyticus
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 4 x CA
Ligand 6NG 1 x 6NG
Ligand GOL 2 x GOL
Ligand DMS 3 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6122
Unit cell:
a: 92.528Å b: 92.528Å c: 131.314Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.104 0.103 0.121

Quick links

Citations

3 review citations

The Molecular Origin of Enthalpy/Entropy Compensation in Biomolecular Recognition.
Fox et al. (2018)
2 more