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PDBsum entry 4a0c
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1155 a.a.
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692 a.a.
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89 a.a.
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80 a.a.
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PDB id:
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Cell cycle
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Title:
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Structure of the cand1-cul4b-rbx1 complex
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Structure:
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Cullin-associated nedd8-dissociated protein 1. Chain: a, b. Synonym: cullin-associated and neddylation-dissociated protein 1, tbp-interacting protein of 120 kda a, tbp-interacting protein 120a, p120 cand1. Engineered: yes. Cullin-4b. Chain: c, e. Synonym: cul-4b.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five. Mus musculus. House mouse. Organism_taxid: 10090.
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Resolution:
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3.80Å
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R-factor:
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0.242
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R-free:
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0.319
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Authors:
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A.Scrima,E.S.Fischer,M.Faty,H.Gut,N.H.Thoma
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Key ref:
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E.S.Fischer
et al.
(2011).
The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation.
Cell,
147,
1024-1039.
PubMed id:
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Date:
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08-Sep-11
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Release date:
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30-Nov-11
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PROCHECK
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Headers
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References
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Q86VP6
(CAND1_HUMAN) -
Cullin-associated NEDD8-dissociated protein 1 from Homo sapiens
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Seq: Struc:
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1230 a.a.
1155 a.a.*
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Q13620
(CUL4B_HUMAN) -
Cullin-4B from Homo sapiens
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Seq: Struc:
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913 a.a.
692 a.a.
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Enzyme class 2:
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Chains D, F:
E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Enzyme class 3:
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Chains D, F:
E.C.2.3.2.32
- cullin-RING-type E3 NEDD8 transferase.
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Reaction:
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S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]- L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N6-[NEDD8- protein]-yl-[cullin]-L-lysine
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Cell
147:1024-1039
(2011)
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PubMed id:
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The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation.
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E.S.Fischer,
A.Scrima,
K.Böhm,
S.Matsumoto,
G.M.Lingaraju,
M.Faty,
T.Yasuda,
S.Cavadini,
M.Wakasugi,
F.Hanaoka,
S.Iwai,
H.Gut,
K.Sugasawa,
N.H.Thomä.
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ABSTRACT
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');
}
}
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