› 2tli

X-ray diffraction
1.95Å resolution

THERMOLYSIN (5% ISOPROPANOL SOAKED CRYSTALS)

Released:
DOI: 10.2210/pdb2tli/pdb
PDB entry 2tli coloured by chain, front view.
PDB entry 2tli coloured by chain, side view.
PDB entry 2tli coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol.
English AC, Done SH, Caves LS, Groom CR, Hubbard RE
Proteins 37 628-40 (1999)
PMID: 10651278

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chain: A
Molecule details ›
Chain: A
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

4 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 4 x CA
Ligand DMS 1 x DMS
Ligand IPA 1 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6122
Unit cell:
a: 93.99Å b: 93.99Å c: 130.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.166 0.211

Quick links

Citations

9 review citations

The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential.
Adekoya et al. (2009)
8 more

7 mentions without citation

XFEL diffraction: developing processing methods to optimize data quality.
Sauter NK. (2015)
6 more