Summary for 1OS0
| Entry DOI | 10.2210/pdb1os0/pdb |
| Related | 1KEI 1QF0 1QF1 1QF2 1TLP 2TMN |
| Descriptor | Thermolysin, ZINC ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | thermolysin, alpha-amino phosphinic compound, neprylisin, hydrolase, metal-binding, metalloprotease, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Bacillus thermoproteolyticus |
| Cellular location | Secreted: P00800 |
| Total number of polymer chains | 1 |
| Total formula weight | 35160.68 |
| Authors | Selkti, M.,Tomas, A.,Prange, T. (deposition date: 2003-03-18, release date: 2003-03-25, Last modification date: 2023-08-16) |
| Primary citation | Selkti, M.,Tomas, A.,Gaucher, J.F.,Prange, T.,Fournie-Zaluski, M.C.,Chen, H.,Roques, B.P. Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition. Acta Crystallogr.,Sect.D, 59:1200-1205, 2003 Cited by PubMed Abstract: A new alpha-aminophosphinic compound able to inhibit both zinc-containing exopeptidases and endopeptidases has been crystallized with TLN as a model in order to investigate the mode of zinc recognition by the phosphinic moiety and to evaluate the potential role of the free alpha-amino group in the formation of enzyme-inhibitor complexes. In addition to the main interactions between the backbone of the inhibitor and the enzyme active site, it is observed that the phosphinic group acts as a distorted bidentate ligand for the zinc ion, while the free alpha-amino function does not directly participate in interactions within the active site. Association of the present data and the K(i) values of various analogues of the inhibitor towards TLN and neprilysin suggests differences in the hydrophobicity of the S(1)-S(2) domains of the enzymes. This could be taken into account in the design of selective inhibitors. PubMed: 12832763DOI: 10.1107/S0907444903010060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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