2wlw
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wlw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Macaca_mulatta Macaca mulatta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WLW FirstGlance]. <br> | <table><tr><td colspan='2'>[[2wlw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Macaca_mulatta Macaca mulatta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WLW FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wlv|2wlv]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wlv|2wlv]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wlw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wlw RCSB], [http://www.ebi.ac.uk/pdbsum/2wlw PDBsum]</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=2wlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wlw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wlw RCSB], [http://www.ebi.ac.uk/pdbsum/2wlw PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/B1P761_MACMU B1P761_MACMU]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 33: | ||
[[Category: Macaca mulatta]] | [[Category: Macaca mulatta]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: James, L C | + | [[Category: James, L C]] |
| - | [[Category: Lammers, M | + | [[Category: Lammers, M]] |
| - | [[Category: Marzetta, F | + | [[Category: Marzetta, F]] |
| - | [[Category: Price, A J | + | [[Category: Price, A J]] |
| - | [[Category: Schaller, T | + | [[Category: Schaller, T]] |
| - | [[Category: Towers, G J | + | [[Category: Towers, G J]] |
| - | [[Category: Wilson, S J | + | [[Category: Wilson, S J]] |
| - | [[Category: Ylinen, L M.J | + | [[Category: Ylinen, L M.J]] |
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Rhesus macaque trim-cyp]] | [[Category: Rhesus macaque trim-cyp]] | ||
[[Category: Rotamase]] | [[Category: Rotamase]] | ||
Revision as of 11:03, 25 December 2014
STRUCTURE OF THE N-TERMINAL CAPSID DOMAIN OF HIV-2
| |||||||||||
