1fjo

THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)

spinqualitylabelsall models 1fjo, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fjo is a 1 chain structure with sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACN, CA, DMS, ZN Related: 1tli, 2tli, 3tli, 4tli, 5tli, 6tli, 7tli, 8tli, 1fj3, 1fjq, 1fjt, 1fju, 1fjv, 1fjw Activity: Thermolysin, with EC number 3.4.24.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [THER_BACTH] Extracellular zinc metalloprotease. 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 Multiple Solvent Crystal Structures (MSCS) is a crystallographic technique to identify energetically favorable positions and orientations of small organic molecules on the surface of proteins. We determined the high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 50--70% acetone, 50--80% acetonitrile and 50 mM phenol. The structures of the protein in the aqueous-organic mixtures are essentially the same as the native enzyme and a number of solvent interaction sites were identified. The distribution of probe molecules shows clusters in the main specificity pocket of the active site and a buried subsite. Within the active site, we compared the experimentally determined solvent positions with predictions from two computational functional group mapping techniques, GRID and Multiple Copy Simultaneous Search (MCSS). The experimentally determined small molecule positions are consistent with the structures of known protein--ligand complexes of TLN. Experimental and computational mapping of the binding surface of a crystalline protein.,English AC, Groom CR, Hubbard RE Protein Eng. 2001 Jan;14(1):47-59. PMID:11287678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thermolysin

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