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The structural basis for site-specific lysine-acetylated histone recognition by the bromodomains of the human transcriptional co- activators pcaf and cbp

Analyse The structural basis for site-specific lysine-acetylated histone recognition by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RNW
Type
protein
Length
133 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone acetyltransferase pcaf; Histone H3
EC
2.3.1.48
UniProt
Q92831, P61830

Structure

solution nmr · 2 distinct chains · 50% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase pcaf (EC 2.3.1.48)protein11857% helix, 0% strandQ92831
BHistone H3protein150% helix, 0% strandP61830

Interfaces

1 interface between chains.

  • A–B · 674 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 2RNW · The Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92831 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT2B (Q92831) · a predicted model of the same protein · chain A against A, TM-score 0.83
  • P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain B against A, TM-score 0.23

Analyse

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