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8HAK

Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 4 (4.5 angstrom resolution)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, E
(A, E)
Histone H3.1polymer13515306.02UniProt (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 H4polymer10211345.32Pfam (PF15511)
UniProt (by SIFTS) (P62805)
Homo sapiens
3C, G
(C, G)
Histone H2A type 1-B/Epolymer12914034.42UniProt (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-Jpolymer12513804.02UniProt (P06899)
Pfam (PF00125)
Homo sapiens (human)Histone H2B.1,Histone H2B.r,H2B/r
5I, J
(J, K)
DNA (180-mer)polymer18055560.52Homo sapiens
6K
(N)
Histone acetyltransferase p300polymer79692314.41UniProt (Q09472)
Pfam (PF02135)
Pfam (PF00439)
Pfam (PF06001)
Pfam (PF08214)
Pfam (PF00569)
Homo sapiens (human)p300 HAT,E1A-associated protein p300,Histone butyryltransferase p300,Histone crotonyltransferase p300,Protein 2-hydroxyisobutyryltransferase p300,Protein lactyltransferas p300,Protein propionyltransferase p300
Sequence modifications
N: 1048 - 1836 (UniProt: Q09472)
PDBExternal DatabaseDetails
Gly 1041-expression tag
Ser 1042-expression tag
Ser 1043-expression tag
Gly 1044-expression tag
Ser 1045-expression tag
Ser 1046-expression tag
Gly 1047-expression tag
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains11
Total formula weight312414.8
All*Total formula weight312414.8
*Water molecules are not included.

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PDB entries from 2025-06-11

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