› 6tmn

X-ray diffraction
1.6Å resolution

Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond

Released:
DOI: 10.2210/pdb6tmn/pdb
PDB entry 6tmn coloured by chain, front view.
PDB entry 6tmn coloured by chain, side view.
PDB entry 6tmn coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.
Tronrud DE, Holden HM, Matthews BW
Science 235 571-4 (1987)
PMID: 3810156

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
Expression system: Not provided
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 0PI 1 x 0PI
Ligand CA 4 x CA
Ligand ZN 1 x ZN
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
0.171 not available not available
Expression system: Not provided

Quick links

Citations

13 review citations

Structural insights into translational fidelity.
Ogle et al. (2005)
12 more

8 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
7 more