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4odq

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==Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide==
==Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide==
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<StructureSection load='4odq' size='340' side='right' caption='[[4odq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4odq' size='340' side='right'caption='[[4odq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4odq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ODQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4odq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ODQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ODQ FirstGlance]. <br>
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</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4odk|4odk]], [[4odl|4odl]], [[4odm|4odm]], [[4odn|4odn]], [[4odo|4odo]], [[4odp|4odp]], [[4odr|4odr]]</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=4odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4odq OCA], [https://pdbe.org/4odq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4odq RCSB], [https://www.ebi.ac.uk/pdbsum/4odq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4odq ProSAT]</span></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='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=4odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4odq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4odq RCSB], [http://www.ebi.ac.uk/pdbsum/4odq PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RS3_ECOLI RS3_ECOLI]] Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity).<ref>PMID:15652481</ref> Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.<ref>PMID:15652481</ref>
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[https://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</ref> [https://www.uniprot.org/uniprot/Q5SLE7_THET8 Q5SLE7_THET8]
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==See Also==
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Low, C]]
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[[Category: Homo sapiens]]
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[[Category: Nordlund, P]]
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[[Category: Large Structures]]
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[[Category: Quistgaard, E M]]
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[[Category: Thermus thermophilus]]
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[[Category: Chaperone]]
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[[Category: Low C]]
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[[Category: Fkbp domain]]
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[[Category: Nordlund P]]
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[[Category: Isomerase]]
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[[Category: Quistgaard EM]]
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[[Category: Peptidyl-prolyl isomerase]]
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[[Category: Ppiase]]
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Current revision

Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide

PDB ID 4odq

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