› 1z9g

X-ray diffraction
1.7Å resolution

Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-retro-thiorphan

Released:
DOI: 10.2210/pdb1z9g/pdb
PDB entry 1z9g coloured by chain, front view.
PDB entry 1z9g coloured by chain, side view.
PDB entry 1z9g coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin.
Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW
Biochemistry 28 1493-7 (1989)
PMID: 2719912

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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P6122
Unit cell:
a: 94Å b: 94Å c: 132Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 not available

Quick links

Citations

4 review citations

Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs.
Böhm HJ. (1998)
3 more

4 mentions without citation

Assessment of programs for ligand binding affinity prediction.
Kim et al. (2008)
3 more