4fjv: Difference between revisions

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'''Unreleased structure'''


The entry 4fjv is ON HOLD
==Crystal Structure of Human Otubain2 and Ubiquitin Complex==
<StructureSection load='4fjv' size='340' side='right'caption='[[4fjv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fjv]] 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=4FJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.047&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEH:ETHANAMINE'>NEH</scene></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=4fjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjv OCA], [https://pdbe.org/4fjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjv RCSB], [https://www.ebi.ac.uk/pdbsum/4fjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OTUB2_HUMAN OTUB2_HUMAN] Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.<ref>PMID:12704427</ref> <ref>PMID:18954305</ref>


Authors: Altun, M., Walter, T.S., Kramer, H.B., Iphofer, A., David, Y., Komsany, A., Ternette, N., Nicholson, B., Navon, A., Stuart, D.I., Ren, J., Kessler, B.M.
==See Also==
 
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
Description: Crystal Structure of Human Otubain2 and Ubiquitin Complex
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Altun M]]
[[Category: David Y]]
[[Category: Iphofer A]]
[[Category: Kessler BM]]
[[Category: Komsany A]]
[[Category: Kramer HB]]
[[Category: Navon A]]
[[Category: Nicholson B]]
[[Category: Ren J]]
[[Category: Stuart DI]]
[[Category: Ternette N]]
[[Category: Walter TS]]

Latest revision as of 18:26, 14 March 2024

Crystal Structure of Human Otubain2 and Ubiquitin ComplexCrystal Structure of Human Otubain2 and Ubiquitin Complex

Structural highlights

4fjv 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 2.047Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OTUB2_HUMAN Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.[1] [2]

See Also

References

  1. Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep. 2003 May;4(5):517-22. PMID:12704427 doi:10.1038/sj.embor.embor824
  2. Edelmann MJ, Iphofer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM. Structural basis and specificity of human otubain 1-mediated deubiquitination. Biochem J. 2009 Mar 1;418(2):379-90. PMID:18954305 doi:10.1042/BJ20081318

4fjv, resolution 2.05Å

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