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==Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99A==
==Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99A==
<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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[2kfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><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>
<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'>[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.  
[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra C]]
[[Category: Bountra, C]]
[[Category: Davis T]]
[[Category: Davis, T]]
[[Category: Dhe-Paganon S]]
[[Category: Dhe-Paganon, S]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Fares C]]
[[Category: Fares, C]]
[[Category: Gutmanas A]]
[[Category: Gutmanas, A]]
[[Category: Lemak A]]
[[Category: Lemak, A]]
[[Category: Li Y]]
[[Category: Li, Y]]
[[Category: Ouyang H]]
[[Category: Structural genomic]]
[[Category: Sunnerhagen M]]
[[Category: Ouyang, H]]
[[Category: Weigelt J]]
[[Category: Sunnerhagen, M]]
[[Category: Weigelt, J]]
[[Category: Fkbp3-n]]
[[Category: Isomerase]]
[[Category: Nesg]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: PSI, Protein structure initiative]]
[[Category: Rotamase]]
[[Category: Sgc]]

Revision as of 11:44, 14 June 2023

Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99AStructure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99A

Structural highlights

2kfv is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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