1BQB
AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE
Summary for 1BQB
| Entry DOI | 10.2210/pdb1bqb/pdb |
| Descriptor | PROTEIN (AUREOLYSIN), ZINC ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, metalloproteinase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 33544.43 |
| Authors | Medrano, F.J.,Banbula, A.,Potempa, J.,Travis, J.,Bode, W. (deposition date: 1998-07-14, release date: 1999-01-13, Last modification date: 2023-08-09) |
| Primary citation | Banbula, A.,Potempa, J.,Travis, J.,Fernandez-Catalan, C.,Mann, K.,Huber, R.,Bode, W.,Medrano, F. Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution. Structure, 6:1185-1193, 1998 Cited by PubMed Abstract: Aureolysin is an extracellular zinc-dependent metalloproteinase from the pathogenic bacterium Staphylococcus aureus. This enzyme exhibits in vitro activity against several molecules of biological significance for the host, indicating that it is involved in the pathology of staphylococcal diseases. PubMed: 9753696DOI: 10.1016/S0969-2126(98)00118-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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