2pbc: Difference between revisions

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<StructureSection load='2pbc' size='340' side='right'caption='[[2pbc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2pbc' size='340' side='right'caption='[[2pbc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pbc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBC FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pbc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP2, FKBP13 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=2pbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbc OCA], [https://pdbe.org/2pbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbc RCSB], [https://www.ebi.ac.uk/pdbsum/2pbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbc ProSAT]</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=2pbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbc OCA], [https://pdbe.org/2pbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbc RCSB], [https://www.ebi.ac.uk/pdbsum/2pbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FKBP2_HUMAN FKBP2_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.  
[https://www.uniprot.org/uniprot/FKBP2_HUMAN FKBP2_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
== 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: Bochkarev A]]
[[Category: Bochkarev, A]]
[[Category: Butler-Cole C]]
[[Category: Butler-Cole, C]]
[[Category: Davis T]]
[[Category: Davis, T]]
[[Category: Dhe-Paganon S]]
[[Category: Dhe-Paganon, S]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Neculai D]]
[[Category: Neculai, D]]
[[Category: Sicheri F]]
[[Category: Structural genomic]]
[[Category: Sundstrom M]]
[[Category: Sicheri, F]]
[[Category: Walker JR]]
[[Category: Sundstrom, M]]
[[Category: Weigelt J]]
[[Category: Walker, J R]]
[[Category: Weigelt, J]]
[[Category: Endoplasmic reticulum]]
[[Category: Isomerase]]
[[Category: Polymorphism]]
[[Category: Rotamase]]
[[Category: Sgc]]

Latest revision as of 13:58, 30 August 2023

FK506-binding protein 2FK506-binding protein 2

Structural highlights

2pbc is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FKBP2_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Evolutionary Conservation

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

See Also

2pbc, resolution 1.80Å

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