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Structure paper

TitleDissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 52, Page 1822-1828, Year 2013
Publish dateSep 18, 2012 (structure data deposition date)
AuthorsBiela, A. / Nasief, N.N. / Betz, M. / Heine, A. / Hangauer, D. / Klebe, G.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:23283700
MethodsX-ray diffraction
Resolution1.56 Å
Structure data

PDB-4h57:
Thermolysin inhibition
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-0PJ:
N-[(S)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-L-leucyl-L-leucine

ChemComp-GOL:
GLYCEROL

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

Source
  • bacillus thermoproteolyticus (bacteria)
KeywordsHYDROLASE/HYDROLASE inhibitor / PROTEASE PHOSPHONAMIDATE INHIBITOR / METAL-BINDING / METALLOPROTEASE / PROTEASE / SECRETED / HYDROLASE-HYDROLASE inhibitor complex

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