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PDBsum entry 1yla
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* Residue conservation analysis
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PDB id:
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Ligase
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Title:
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Ubiquitin-conjugating enzyme e2-25 kda (huntington interacting protein 2)
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Structure:
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Ubiquitin-conjugating enzyme e2-25 kda. Chain: a, b. Synonym: ubiquitin- protein ligase, ubiquitin carrier protein, e225k, huntingtin interacting protein 2, hip-2. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hip2, lig. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.40Å
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R-factor:
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0.225
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R-free:
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0.269
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Authors:
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J.Choe,G.V.Avvakumov,E.M.Newman,F.Mackenzie,I.Kozieradzki, A.Bochkarev,M.Sundstrom,C.Arrowsmith,A.Edwards,S.Dhe-Paganon, Structural Genomics Consortium (Sgc)
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Key ref:
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S.Ko
et al.
(2010).
Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity.
J Biol Chem,
285,
36070-36080.
PubMed id:
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Date:
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19-Jan-05
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Release date:
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01-Feb-05
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PROCHECK
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Headers
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References
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P61086
(UBE2K_HUMAN) -
Ubiquitin-conjugating enzyme E2 K from Homo sapiens
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Seq: Struc:
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200 a.a.
201 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.3.2.23
- E2 ubiquitin-conjugating enzyme.
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Reaction:
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine
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J Biol Chem
285:36070-36080
(2010)
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PubMed id:
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Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity.
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S.Ko,
G.B.Kang,
S.M.Song,
J.G.Lee,
D.Y.Shin,
J.H.Yun,
Y.Sheng,
C.Cheong,
Y.H.Jeon,
Y.K.Jung,
C.H.Arrowsmith,
G.V.Avvakumov,
S.Dhe-Paganon,
Y.J.Yoo,
S.H.Eom,
W.Lee.
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ABSTRACT
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');
}
}
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