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-Structure paper
Title | Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition. |
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Journal, issue, pages | Acta Crystallogr. ,Sect. D, Vol. 59, Page 1200-1205, Year 2003 |
Publish date | Mar 18, 2003 (structure data deposition date) |
Authors | Selkti, M. / Tomas, A. / Gaucher, J.F. / Prange, T. / Fournie-Zaluski, M.C. / Chen, H. / Roques, B.P. |
External links | Acta Crystallogr. ,Sect. D / PubMed:12832763 |
Methods | X-ray diffraction |
Resolution | 2.1 Å |
Structure data | PDB-1os0: |
Chemicals | ChemComp-ZN: ChemComp-CA: ChemComp-0PQ: ChemComp-DMS: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / THERMOLYSIN / ALPHA-AMINO PHOSPHINIC COMPOUND / NEPRYLISIN / HYDROLASE / Metal-binding / Metalloprotease / Protease / Secreted / Zymogen / HYDROLASE-HYDROLASE INHIBITOR complex |