2e3x

Crystal structure of Russell's viper venom metalloproteinase

spinqualitylabelsall models 2e3x, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2e3x is a 3 chain structure with sequence from Daboia russellii siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GM6, NAG, ZN, MAN Activity: Russellysin, with EC number 3.4.24.58 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VM3CX_DABSI] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. [SLLC1_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner. [SLLC2_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases.,Takeda S, Igarashi T, Mori H FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA