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2kfv
From Proteopedia
(Difference between revisions)
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<StructureSection load='2kfv' size='340' side='right'caption='[[2kfv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2kfv' size='340' side='right'caption='[[2kfv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2kfv]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2kfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KFV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP25, FKBP3 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP25, FKBP3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfv OCA], [https://pdbe.org/2kfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kfv RCSB], [https://www.ebi.ac.uk/pdbsum/2kfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kfv ProSAT], [https://www.topsan.org/Proteins/NESGC/2kfv TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/FKBP3_HUMAN FKBP3_HUMAN]] FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[ | + | *[[FKBP 3D structures|FKBP 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:04, 1 December 2021
Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99A
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Categories: Human | Large Structures | Peptidylprolyl isomerase | Arrowsmith, C H | Bountra, C | Davis, T | Dhe-Paganon, S | Edwards, A | Fares, C | Gutmanas, A | Lemak, A | Li, Y | Structural genomic | Ouyang, H | Sunnerhagen, M | Weigelt, J | Fkbp3-n | Isomerase | Nesg | Nucleus | Phosphoprotein | PSI, Protein structure initiative | Rotamase | Sgc
