1BMA
BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE
Summary for 1BMA
Entry DOI | 10.2210/pdb1bma/pdb |
Related PRD ID | PRD_000358 |
Descriptor | Chymotrypsin-like elastase family member 1, CALCIUM ION, SULFATE ION, ... (5 entities in total) |
Functional Keywords | serine protease, metal-binding, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Sus scrofa (pigs,swine,wild boar) |
Cellular location | Secreted: P00772 |
Total number of polymer chains | 1 |
Total formula weight | 26585.77 |
Authors | Peisach, E.,Casebier, D.,Gallion, S.L.,Furth, P.,Petsko, G.A.,Hogan Jr., J.C.,Ringe, D. (deposition date: 1995-05-01, release date: 1995-12-07, Last modification date: 2024-10-23) |
Primary citation | Peisach, E.,Casebier, D.,Gallion, S.L.,Furth, P.,Petsko, G.A.,Hogan Jr., J.C.,Ringe, D. Interaction of a peptidomimetic aminimide inhibitor with elastase. Science, 269:66-69, 1995 Cited by PubMed Abstract: The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design. PubMed: 7604279PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report