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8SN8

Cryo-EM structure of the human nucleosome core particle in complex with RNF168 and UbcH5c~Ub (UbcH5c chemically conjugated to histone H2A) (class 6)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, E
(A, E)
Histone H3.1polymer14015786.52UniProt (P68431)
Pfam (PF00125)
Homo sapiens (human)Histone H3/a,Histone H3/b,Histone H3/c,Histone H3/d,Histone H3/f,Histone H3/h,Histone H3/i,Histone H3/j,Histone H3/k,Histone H3/l
2B, F
(B, F)
Histone H4polymer10711743.82UniProt (P62805)
Pfam (PF15511)
Homo sapiens (human)
3C, G
(C, G)
Histone H2A type 1-B/Epolymer11913008.22UniProt (P04908)
Pfam (PF00125)
Pfam (PF16211)
Homo sapiens (human)Histone H2A.2,Histone H2A/a,Histone H2A/m
4D, H
(D, H)
Histone H2B type 1-Jpolymer12814084.32UniProt (P06899)
Pfam (PF00125)
Homo sapiens (human)Histone H2B.1,Histone H2B.r,H2B/r
5I
(I)
DNA (147-MER)polymer14745138.81Homo sapiens
6J
(J)
DNA (147-MER)polymer14745610.01Homo sapiens
7K
(K)
E3 ubiquitin-protein ligase RNF168polymer10311904.01UniProt (Q8IYW5)
Pfam (PF14447)
Homo sapiens (human)hRNF168,RING finger protein 168,RING-type E3 ubiquitin transferase RNF168
8L
(L)
Ubiquitin-conjugating enzyme E2 D3polymer15117061.41UniProt (P61077)
Pfam (PF00179)
Homo sapiens (human)(E3-independent) E2 ubiquitin-conjugating enzyme D3,E2 ubiquitin-conjugating enzyme D3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protein ligase D3
9M
(M)
Polyubiquitin-Bpolymer819057.41UniProt (P0CG47)
Pfam (PF00240)
Homo sapiens (human)
10N, O
(K)
ZINC IONnon-polymer65.42Chemie (ZN)
Sequence modifications
A, E: 0 - 135 (UniProt: P68431)
PDBExternal DatabaseDetails
Gly -4-expression tag
Pro -3-expression tag
Gly -2-expression tag
His -1-expression tag
B, F: 0 - 102 (UniProt: P62805)
PDBExternal DatabaseDetails
Gly -4-expression tag
Pro -3-expression tag
Gly -2-expression tag
His -1-expression tag
C, G: 11 - 129 (UniProt: P04908)
PDBExternal DatabaseDetails
Ser 11Arg 12engineered mutation
Cys 15Lys 16engineered mutation
D, H: 0 - 123 (UniProt: P06899)
PDBExternal DatabaseDetails
Gly -4-expression tag
Pro -3-expression tag
Gly -2-expression tag
His -1-expression tag
K: 1 - 93 (UniProt: Q8IYW5)
PDBExternal DatabaseDetails
Met -9-initiating methionine
Gly -8-expression tag
His -7-expression tag
His -6-expression tag
His -5-expression tag
His -4-expression tag
His -3-expression tag
His -2-expression tag
Gly -1-expression tag
Ser 0-expression tag
L: 1 - 147 (UniProt: P61077)
PDBExternal DatabaseDetails
Gly -3-expression tag
Pro -2-expression tag
Gly -1-expression tag
His 0-expression tag
Ile 21Cys 21engineered mutation
Ala 107Cys 107engineered mutation
Asp 111Cys 111engineered mutation
Lys 119Leu 119engineered mutation
M: 18 - 76 (UniProt: P0CG47)
PDBExternal DatabaseDetails
Gly -4-expression tag
Pro -3-expression tag
Gly -2-expression tag
His -1-expression tag
Met 0-expression tag
Met 1-expression tag
Gln 2-expression tag
Ile 3-expression tag
Phe 4-expression tag
Val 5-expression tag
Lys 6-expression tag
Thr 7-expression tag
Leu 8-expression tag
Thr 9-expression tag
Gly 10-expression tag
Lys 11-expression tag
Thr 12-expression tag
Ile 13-expression tag
Thr 14-expression tag
Leu 15-expression tag
Glu 16-expression tag
Val 17-expression tag
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains13
Total formula weight238017.3
Non-Polymers*Number of molecules2
Total formula weight130.8
All*Total formula weight238148.1
*Water molecules are not included.

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PDB entries from 2024-11-06

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