2mlz

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==NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471==
==NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471==
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<StructureSection load='2mlz' size='340' side='right' caption='[[2mlz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2mlz' size='340' side='right'caption='[[2mlz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mlz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Escherichia_coli_str._k-12_substr._mc4100 Escherichia coli str. k-12 substr. mc4100]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._k-12_substr._mc4100 Escherichia coli str. k-12 substr. mc4100]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLZ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mly|2mly]], [[2mlx|2mlx]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mly|2mly]], [[2mlx|2mlx]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, BN896_0318 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100]), phoA, b0383, JW0374 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, BN896_0318 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100]), phoA, b0383, JW0374 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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<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=2mlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlz OCA], [http://pdbe.org/2mlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mlz RCSB], [http://www.ebi.ac.uk/pdbsum/2mlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlz ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlz OCA], [https://pdbe.org/2mlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlz RCSB], [https://www.ebi.ac.uk/pdbsum/2mlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[[https://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]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Alkaline phosphatase|Alkaline phosphatase]]
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*[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Ecoli]]
[[Category: Ecoli]]
[[Category: Escherichia coli str. k-12 substr. mc4100]]
[[Category: Escherichia coli str. k-12 substr. mc4100]]
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[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Economou, A]]
[[Category: Economou, A]]

Revision as of 15:17, 2 June 2021

NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471

PDB ID 2mlz

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