2E3X
Crystal structure of Russell's viper venom metalloproteinase
Summary for 2E3X
| Entry DOI | 10.2210/pdb2e3x/pdb |
| Descriptor | Coagulation factor X-activating enzyme heavy chain, Coagulation factor X-activating enzyme light chain 2, Coagulation factor X-activating enzyme light chain 1, ... (9 entities in total) |
| Functional Keywords | disintegrin, metalloproteinase, c-type lectin, hydrolase, blood clotting, toxin |
| Biological source | Daboia russellii siamensis More |
| Total number of polymer chains | 3 |
| Total formula weight | 80291.46 |
| Authors | Igarashi, T.,Takeda, S. (deposition date: 2006-11-30, release date: 2007-12-11, Last modification date: 2024-10-23) |
| Primary citation | Takeda, S.,Igarashi, T.,Mori, H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. Febs Lett., 581:5859-5864, 2007 Cited by PubMed Abstract: Russell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 A resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases. PubMed: 18060879DOI: 10.1016/j.febslet.2007.11.062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
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