8GUJ

Bre1-nucleosome complex (Model II)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.80 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Structure of the human Bre1 complex bound to the nucleosome

Onishi, S.Uchiyama, K.Sato, K.Okada, C.Kobayashi, S.Hamada, K.Nishizawa, T.Ogata, K.Sengoku, T.

To be published.

Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H3.1
A, E
136Homo sapiensMutation(s): 0 
Gene Names: 
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Find proteins for P68431 (Homo sapiens)
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UniProt GroupP68431
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H4
B, F
102Homo sapiensMutation(s): 0 
Gene Names: 
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Find proteins for P62805 (Homo sapiens)
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UniProt GroupP62805
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H2A type 1
C, G
129Homo sapiensMutation(s): 0 
Gene Names: 
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UniProt GroupP0C0S8
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H2B type 1-J
D, H
129Homo sapiensMutation(s): 0 
Gene Names: H2BC11H2BFRHIST1H2BJ
UniProt & NIH Common Fund Data Resources
Find proteins for P06899 (Homo sapiens)
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
E3 ubiquitin-protein ligase BRE1A975Homo sapiensMutation(s): 0 
Gene Names: RNF20BRE1A
EC: 2.3.2.27
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Find proteins for Q5VTR2 (Homo sapiens)
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
E3 ubiquitin-protein ligase BRE1B1,001Homo sapiensMutation(s): 0 
Gene Names: RNF40BRE1BKIAA0661
EC: 2.3.2.27
UniProt & NIH Common Fund Data Resources
Find proteins for O75150 (Homo sapiens)
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Entity ID: 5
MoleculeChains LengthOrganismImage
DNA (147-mer)147synthetic construct
Sequence Annotations
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Entity ID: 6
MoleculeChains LengthOrganismImage
DNA (147-mer)147synthetic construct
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.80 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Japan Society for the Promotion of Science (JSPS)Japan--

Revision History  (Full details and data files)

  • Version 1.0: 2023-09-20
    Type: Initial release