› 1thl

X-ray diffraction
1.7Å resolution

Thermolysin complexed with a novel glutaramide derivative, n-(1-(2(r,s)-carboxy-4-phenylbutyl) cyclopentylcarbonyl)-(s)-tryptophan

Released:
DOI: 10.2210/pdb1thl/pdb
PDB entry 1thl coloured by chain, front view.
PDB entry 1thl coloured by chain, side view.
PDB entry 1thl coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex.
Holland DR, Barclay PL, Danilewicz JC, Matthews BW, James K
Biochemistry 33 51-6 (1994)
PMID: 8286362

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

3 bound ligands:
Ligand CA 4 x CA
Ligand ZN 1 x ZN
Ligand 0DB 1 x 0DB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
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
0.162 0.162 not available

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Citations

1 review citation

The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential.
Adekoya et al. (2009)
6 other articles

12 mentions without citation

BRCA1 and homologous recombination: implications from mouse embryonic development.
Liu et al. (2020)
11 more