2vb1 | pdb_00002vb1

HEWL at 0.65 angstrom resolution

spinqualitylabelsall models 2vb1, resolution 0.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vb1 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, EDO, NO3 Related: 1aki, 1azf, 1b2k, 1bgi, 1bvx, 1bwj, 1c10, 1dpw, 1dqj, 1f0w, 1f10, 1fdl, 1flq, 1flu, 1flw, 1fn5, 1g7i, 1g7l, 1gwd, 1gxv, 1h6m, 1hc0, 1hel, 1hen, 1heo, 132l, 193l, 194l, 1a2y, 1at5, 1at6, 1b0d, 1bhz, 1bvk, 1bwh, 1bwi, 1c08, 1dpx, 1e8l, 1f3j, 1fly, 1g7h, 1g7j, 1g7m, 1gpq, 1gxx, 1h87, 1hem, 1heq, 1her, 1hsw, 1hep, 1hew, 1hf4, 1ic4, 1ic5, 1ic7, 1iee, 1io5, 1ioq, 1ios, 1iot, 1ir7, 1ir9, 1j1x, 1ja2, 1ja6, 1jis, 1jit, 1jj0, 1jj1, 1jj3, 1kip, 1kir, 1lcn, 1hsx, 1ior, 1ir8, 1j1o, 1j1p, 1ja4, 1ja7, 1jiy, 1jpo, 1jto, 1jtt, 1kiq, 1kxw, 1kxx, 1kxy, 1lj3, 1lj4, 1ljf, 1ljh, 1ljj, 1ljk, 1lkr, 1lks, 1lpi, 1lsa, 1lse, 1lje, 1ljg, 1lji, 1lma, 1lsb, 1lsc, 1lsd, 1lsf, 1lsm, 1lsn, 1lsy, 1lys, 1lz9, 1lzc, 1lze, 1lzg, 1lzh, 1mel, 1n4f, 1nby, 1ndg, 1qio, 1ri8, 1rjc, 1sf6, 1sfg, 1lsg, 1lsz, 1lyo, 1lyz, 1lz8, 1lza, 1lzb, 1lzd, 1lzn, 1lzt, 1mlc, 1nbz, 1ndm, 1p2c, 1ps5, 1qtk, 1rcm, 1rfp, 1sf4, 1sf7, 1sfb, 1sq2, 1t3p, 1t6v, 1ua6, 1uc0, 1uco, 1uib, 1uif, 1vat, 1vdp, 1vds, 1vdt, 1ved, 1vfb, 1w6z, 1wtm, 1wtn, 1xej, 1xgq, 1yik, 1ykx, 1yl0, 1yqv, 1zmy, 2aub, 2bly, 2bpu, 1uia, 1uic, 1uid, 1uie, 1uig, 1uih, 1uuz, 1v7s, 1v7t, 1vau, 1vdq, 1xei, 1xek, 1xfp, 1xgp, 1yil, 1yky, 1ykz, 1yl1, 1z55, 2a6u, 2a7d, 2a7f, 2b5z, 2blx, 2c8o, 2c8p, 2cds, 2d4i, 2d6b, 2d91, 2lyo, 3hfm, 3lyt, 3lyz, 4lyo, 5lyz, 6lyt, 6lyz, 7lyz, 8lyz, 2cgi, 2d4j, 2d4k, 2fbb, 2hfm, 2iff, 2lym, 2lyz, 2lzh, 2lzt, 3lym, 3lyo, 3lzt, 4lym, 4lyt, 4lyz, 4lzt, 5lym, 5lyt Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. 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 The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation. Refinement with anisotropic displacement parameters and with the removal of stereochemical restraints for the well ordered parts of the structure converged with a conventional R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. In addition to the 129-residue protein, a total of 170 water molecules, nine nitrate ions, one acetate ion and three ethylene glycol molecules were located in the electron-density map. Eight sections of the main chain and many side chains were modeled with alternate conformations. The occupancies of the water sites were refined and this step is meaningful when assessed by use of the free R factor. A detailed description and comparison of the structure are made with reference to the previously reported triclinic HEWL structures refined at 0.925 A (at the low temperature of 120 K) and at 0.95 A resolution (at room temperature). Triclinic lysozyme at 0.65 A resolution.,Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1254-68. Epub 2007, Nov 16. PMID:18084073 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

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