| Structural highlights
1gwd is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Related: | 132l, 193l, 194l, 1a2y, 1aki, 1at5, 1at6, 1azf, 1b0d, 1b2k, 1bgi, 1bhz, 1bvk, 1bvx, 1bwh, 1bwi, 1bwj, 1c08, 1c10, 1dpw, 1dpx, 1dqj, 1e8l, 1f0w, 1f10, 1f3j, 1fdl, 1flq, 1flu, 1flw, 1fly, 1fn5, 1g7h, 1g7i, 1g7j, 1g7l, 1g7m, 1gpq, 1h6m, 1h87, 1hc0, 1hel, 1hem, 1hen, 1heo, 1hep, 1heq, 1her, 1hew, 1hf4, 1hsw, 1hsx, 1ic4, 1ic5, 1ic7, 1iee, 1io5, 1ioq, 1ior, 1ios, 1iot, 1ir7, 1ir8, 1ir9, 1ja2, 1ja4, 1ja6, 1ja7, 1jis, 1jit, 1jiy, 1jj0, 1jj1, 1jj3, 1jpo, 1jto, 1kip, 1kiq, 1kir, 1kxw, 1kxx, 1kxy, 1lcn, 1lkr, 1lks, 1lma, 1lpi, 1lsa, 1lsb, 1lsc, 1lsd, 1lse, 1lsf, 1lsg, 1lsm, 1lsn, 1lsy, 1lsz, 1lyo, 1lys, 1lyz, 1lz8, 1lz9, 1lza, 1lzb, 1lzc, 1lzd, 1lze, 1lzg, 1lzh, 1lzn, 1lzt, 1mel, 1mlc, 1qio, 1qtk, 1rcm, 1rfp, 1uco, 1uia, 1uib, 1uic, 1uid, 1uie, 1uif, 1uig, 1uih, 1xei, 1xej, 1xek, 2hfm, 2iff, 2lym, 2lyo, 2lyz, 2lzh, 2lzt, 3hfl, 3hfm, 3lym, 3lyo, 3lyt, 3lyz, 3lzt, 4lym, 4lyo, 4lyt, 4lyz, 4lzt, 5lym, 5lyt, 5lyz, 6lyt, 6lyz, 7lyz, 8lyz |
| Activity: | Lysozyme, with EC number 3.2.1.17 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
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.[1]
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
A series of experiments performed at Cu Kalpha wavelength on in-house X-ray equipment are presented which investigate two possibilities for enhancing the experimental phasing signal by means of (i) triiodide/iodide soaks using KI/I(2) and (ii) combinations of counter-ions introduced using the short cryosoak method. Triiodide-derivative crystal structures for five test proteins have been refined and reveal that iodine can bind as polyiodide and single iodide ions through hydrophobic and hydrogen-bonding interactions both at the molecular surface and in intramolecular and intermolecular cavities. In three cases, the structures could be automatically determined with autoSHARP using in-house SAD and SIRAS data. The investigation of combinatorial counter-ion replacement using multiple salts with Na(+) and Cs(+) as cations and I(-) and Cl(-) as anions reveals that, for the case of hen egg-white lysozyme, significant improvement in phasing signal is obtained by the combined use of salts compared with SIRAS methods using native and single short-soak derivative data sets.
Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment.,Evans G, Bricogne G Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:12037300[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Evans G, Bricogne G. Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:12037300
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