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Solution structure of the isolated histone H2A-H2B heterodimer

Analyse Solution structure of the isolated histone H2A-H2B heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RVQ
Type
protein
Length
262 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone H2A type 1-B/E; Histone H2B type 1-J
UniProt
P04908, P06899
Pockets
1 · best druggability 0.56

Structure

solution nmr · 2 distinct chains · 46% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CHistone H2A type 1-B/Eprotein13341% helix, 2% strandP04908
DHistone H2B type 1-Jprotein12952% helix, 2% strandP06899

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11740.560.8027empty

Interfaces

1 interface between chains.

  • C–D · 2665 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 2RVQ · Solution structure of the isolated histone H2A-H2B heterodimer · the same entry in another collection · chain C against C, TM-score 1.00
  • P06899 · AlphaFold monomer V2.0 prediction for histone H2B type 1-J (P06899) · a predicted model of the same protein · chain D against A, TM-score 0.61
  • P04908 · AlphaFold monomer V2.0 prediction for histone H2A type 1-B/E (P04908) · a predicted model of the same protein · chain C against A, TM-score 0.51

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