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1BMA

BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE

Summary for 1BMA
Entry DOI10.2210/pdb1bma/pdb
Related PRD IDPRD_000358
DescriptorChymotrypsin-like elastase family member 1, CALCIUM ION, SULFATE ION, ... (5 entities in total)
Functional Keywordsserine protease, metal-binding, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceSus scrofa (pigs,swine,wild boar)
Cellular locationSecreted: P00772
Total number of polymer chains1
Total formula weight26585.77
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 citationPeisach, 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: 7604279
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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