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2mly
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mlx|2mlx]], [[2mlz|2mlz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mlx|2mlx]], [[2mlz|2mlz]]</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 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 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=2mly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mly OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mly RCSB], [http://www.ebi.ac.uk/pdbsum/2mly 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=2mly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mly OCA], [http://pdbe.org/2mly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mly RCSB], [http://www.ebi.ac.uk/pdbsum/2mly PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/U6N325_ECOLI U6N325_ECOLI]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity).[RuleBase:RU003914] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).[HAMAP-Rule:MF_00303] | [[http://www.uniprot.org/uniprot/U6N325_ECOLI U6N325_ECOLI]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity).[RuleBase:RU003914] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).[HAMAP-Rule:MF_00303] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2mly" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Alkaline phosphatase|Alkaline phosphatase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:33, 11 September 2015
NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150
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