› 1l3f

X-ray diffraction
2.3Å resolution

Thermolysin in the Absence of Substrate has an Open Conformation

Released:
DOI: 10.2210/pdb1l3f/pdb
PDB entry 1l3f coloured by chain, front view.
PDB entry 1l3f coloured by chain, side view.
PDB entry 1l3f coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Thermolysin in the absence of substrate has an open conformation.
Hausrath AC, Matthews BW
Acta Crystallogr D Biol Crystallogr 58 1002-7 (2002)
PMID: 12037302

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
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P41212
Unit cell:
a: 97.052Å b: 97.052Å c: 106.583Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.302

Quick links

Citations

3 review citations

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

14 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
13 more