1ELB
Analogous inhibitors of elastase do not always bind analogously
Summary for 1ELB
| Entry DOI | 10.2210/pdb1elb/pdb |
| Related | 1ELA 1ELC |
| Related PRD ID | PRD_000368 |
| Descriptor | ELASTASE, 6-ammonio-N-(trifluoroacetyl)-L-norleucyl-N-[4-(1-methylethyl)phenyl]-L-leucinamide, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase-hydrolase inhibitor complex, serine proteinase, hydrolase/hydrolase inhibitor |
| Biological source | Sus scrofa (pig) |
| Cellular location | Secreted: P00772 |
| Total number of polymer chains | 1 |
| Total formula weight | 26537.72 |
| Authors | Mattos, C.,Rasmussen, B.,Ding, X.,Petsko, G.A.,Ringe, D. (deposition date: 1993-12-07, release date: 1994-06-22, Last modification date: 2024-06-05) |
| Primary citation | Mattos, C.,Rasmussen, B.,Ding, X.,Petsko, G.A.,Ringe, D. Analogous inhibitors of elastase do not always bind analogously. Nat.Struct.Biol., 1:55-58, 1994 Cited by PubMed Abstract: It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding--the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites. PubMed: 7656008DOI: 10.1038/nsb0194-55 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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