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9KHT

cryo-EM structure of Ufd2/Ubc4-Ub in complex with K29-linked triUb (dimeric conformation)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, D
(D, d)
Polyubiquitin-Cpolymer768550.82UniProt (P0CG48)
Pfam (PF00240)
Homo sapiens (human)
2B, C, E, F, G...
(E, F, e, f, C...)
Ubiquitinpolymer768576.86UniProt (P62979)
Pfam (PF00240)
Homo sapiens (human)
3I, K
(A, a)
E4 ubiquitin-protein ligase UFD2polymer955109360.72UniProt (P54860)
Pfam (PF10408)
Pfam (PF04564)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)RING-type E3 ubiquitin transferase UFD2,Ubiquitin conjugation factor E4,Ubiquitin fusion degradation protein 2,UB fusion protein 2
4J, L
(B, b)
Ubiquitin-conjugating enzyme E2 4polymer14816442.62UniProt (P15731)
Pfam (PF00179)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)E2 ubiquitin-conjugating enzyme 4,Ubiquitin carrier protein 4,Ubiquitin-protein ligase 4
Sequence modifications
D, d: 1 - 76 (UniProt: P0CG48)
PDBExternal DatabaseDetails
Cys 48Lys 48engineered mutation
B, b: 1 - 148 (UniProt: P15731)
PDBExternal DatabaseDetails
Ser 22Cys 22engineered mutation
Ser 108Cys 108engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains12
Total formula weight320169.2
All*Total formula weight320169.2
*Water molecules are not included.

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PDB entries from 2026-04-01

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