130l: Difference between revisions

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|PDB= 130l |SIZE=350|CAPTION= <scene name='initialview01'>130l</scene>, resolution 1.7&Aring;
|PDB= 130l |SIZE=350|CAPTION= <scene name='initialview01'>130l</scene>, resolution 1.7&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=130l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=130l OCA], [http://www.ebi.ac.uk/pdbsum/130l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=130l RCSB]</span>
}}
}}


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==About this Structure==
==About this Structure==
130L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=130L OCA].  
130L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=130L OCA].  


==Reference==
==Reference==
Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent., Pjura P, Matthews BW, Protein Sci. 1993 Dec;2(12):2226-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8298466 8298466]
Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent., Pjura P, Matthews BW, Protein Sci. 1993 Dec;2(12):2226-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8298466 8298466]
[[Category: Enterobacteria phage t2]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Pjura, P.]]
[[Category: Pjura, P.]]
[[Category: BME]]
[[Category: CL]]
[[Category: hydrolase(o-glycosyl)]]
[[Category: hydrolase(o-glycosyl)]]


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