PDBe 8tln

X-ray diffraction
1.6Å resolution

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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


No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 94.1Å b: 94.1Å c: 131.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 not available not available