› 1lnf

X-ray diffraction
1.7Å resolution

A structural analysis of metal substitutions in thermolysin

Released:
DOI: 10.2210/pdb1lnf/pdb
PDB entry 1lnf coloured by chain, front view.
PDB entry 1lnf coloured by chain, side view.
PDB entry 1lnf coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Structural analysis of zinc substitutions in the active site of thermolysin.
Holland DR, Hausrath AC, Juers D, Matthews BW
Protein Sci 4 1955-65 (1995)
PMID: 8535232

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
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-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
Expression system: Not provided
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand VAL 1 x VAL
Ligand LYS 1 x LYS
Ligand ZN 1 x ZN
Ligand CA 4 x CA
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 93.85Å b: 93.85Å c: 131.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Zinc hydrolases: the mechanisms of zinc-dependent deacetylases.
Hernick et al. (2005)
3 more

5 mentions without citation

Mechanisms of Proteolytic Enzymes and Their Inhibition in QM/MM Studies.
Elsässer et al. (2021)
4 more