› 1fju

X-ray diffraction
2Å resolution

THERMOLYSIN (80% ACETONITRILE SOAKED CRYSTALS)

Released:
DOI: 10.2210/pdb1fju/pdb
PDB entry 1fju coloured by chain, front view.
PDB entry 1fju coloured by chain, side view.
PDB entry 1fju coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Experimental and computational mapping of the binding surface of a crystalline protein.
English AC, Groom CR, Hubbard RE
Protein Eng 14 47-59 (2001)
PMID: 11287678

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: 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 CCN 1 x CCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6122
Unit cell:
a: 93.86Å b: 93.86Å c: 131.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.154 0.205

Quick links

Citations

6 review citations

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

2 mentions without citation

Improving protocols for protein mapping through proper comparison to crystallography data.
Lexa et al. (2013)
1 more