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8SN6

Cryo-EM structure of the human nucleosome core particle in complex with RNF168 and UbcH5c~Ub (UbcH5c chemically conjugated to histone H2A) (class 4)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, EHistone H3.1polymer14015786.52UniProt (P68431)
Pfam (PF00125)
In PDB
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, FHistone H4polymer10711743.82UniProt (P62805)
Pfam (PF15511)
In PDB
Homo sapiens (human)
3C, GHistone H2A type 1-B/Epolymer11913008.22UniProt (P04908)
Pfam (PF00125)
Pfam (PF16211)
In PDB
Homo sapiens (human)Histone H2A.2,Histone H2A/a,Histone H2A/m
4D, HHistone H2B type 1-Jpolymer12814084.32UniProt (P06899)
Pfam (PF00125)
In PDB
Homo sapiens (human)Histone H2B.1,Histone H2B.r,H2B/r
5IDNA (147-MER)polymer14745138.81Homo sapiens
6JDNA (147-MER)polymer14745610.01Homo sapiens
7KE3 ubiquitin-protein ligase RNF168polymer10311904.01UniProt (Q8IYW5)
Pfam (PF14447)
In PDB
Homo sapiens (human)hRNF168,RING finger protein 168,RING-type E3 ubiquitin transferase RNF168
8LUbiquitin-conjugating enzyme E2 D3polymer15117061.41UniProt (P61077)
Pfam (PF00179)
In PDB
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
9MPolyubiquitin-Bpolymer819057.41UniProt (P0CG47)
Pfam (PF00240)
In PDB
Homo sapiens (human)
10KZINC 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 2024-07-24

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