4iav
From Proteopedia
(Difference between revisions)
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- | + | ==G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris with N-Sulfamoyl-L-phenylalanine== | |
- | + | <StructureSection load='4iav' size='340' side='right' caption='[[4iav]], [[Resolution|resolution]] 1.35Å' scene=''> | |
- | + | == Structural highlights == | |
- | ==Function== | + | <table><tr><td colspan='2'>[[4iav]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43649 Atcc 43649]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IAV FirstGlance]. <br> |
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CXA:PHENYLALANINE-N-SULFONAMIDE'>CXA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cpt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2026 ATCC 43649])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_T Carboxypeptidase T], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.18 3.4.17.18] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iav OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iav RCSB], [http://www.ebi.ac.uk/pdbsum/4iav PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/CBPT_THEVU CBPT_THEVU]] Able to split off hydrophobic and basic amino acids with comparable efficiency. | [[http://www.uniprot.org/uniprot/CBPT_THEVU CBPT_THEVU]] Able to split off hydrophobic and basic amino acids with comparable efficiency. | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Carboxypeptidase|Carboxypeptidase]] |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Atcc 43649]] | ||
[[Category: Carboxypeptidase T]] | [[Category: Carboxypeptidase T]] | ||
- | [[Category: Akparov, V K | + | [[Category: Akparov, V K]] |
- | [[Category: Kuranova, I P | + | [[Category: Kuranova, I P]] |
- | [[Category: Kuznetsov, S A | + | [[Category: Kuznetsov, S A]] |
- | [[Category: Timofeev, V I | + | [[Category: Timofeev, V I]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 12:58, 25 December 2014
G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris with N-Sulfamoyl-L-phenylalanine
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