5lbn: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 5lbn is ON HOLD  until Paper Publication
==High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6==
<StructureSection load='5lbn' size='340' side='right'caption='[[5lbn]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lbn]] is a 1 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=5LBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LBN 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]] 1.42&#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></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=5lbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbn OCA], [https://pdbe.org/5lbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lbn RCSB], [https://www.ebi.ac.uk/pdbsum/5lbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UB2E1_HUMAN UB2E1_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.<ref>PMID:16428300</ref> <ref>PMID:20061386</ref>


Authors: Anandapadamanaban, M., Moche, M., Sunnerhagen, M.
==See Also==
 
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
Description: High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Anandapadamanaban, M]]
__TOC__
[[Category: Sunnerhagen, M]]
</StructureSection>
[[Category: Moche, M]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Anandapadamanaban M]]
[[Category: Moche M]]
[[Category: Sunnerhagen M]]

Latest revision as of 15:01, 9 May 2024

High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6

Structural highlights

5lbn is a 1 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 1.42Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UB2E1_HUMAN Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.[1] [2]

See Also

References

  1. Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H. Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. PMID:16428300 doi:10.1093/jb/mvi172
  2. David Y, Ziv T, Admon A, Navon A. The E2 ubiquitin conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Jan 8. PMID:20061386 doi:M109.089003

5lbn, resolution 1.42Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA