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Structure of a human ASF1A-hira complex and insights into specificity of histone chaperone complex assembly

Analyse Structure of a human ASF1A-hira complex and insights into specificity of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2I32
Type
protein
Length
345 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-silencing factor 1 paralog a; Histone regulatory homolog a
UniProt
Q9Y294, P54198
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAnti-silencing factor 1 paralog aprotein15412% helix, 51% strandQ9Y294
EHistone regulatory homolog aprotein210% helix, 48% strandP54198
FHistone regulatory homolog aprotein160% helix, 50% strandP54198

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11450.440.7623empty
2510.240.7216empty

Interfaces

4 interfaces between chains.

  • A–E · 749 Ų buried · 18 hydrogen bonds · protein-protein
  • B–F · 529 Ų buried · 14 hydrogen bonds · protein-protein
  • A–F · 192 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 60 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2I32 · Structure of a human ASF1a-HIRA complex and insights into specificity of histone… · the same entry in another collection · chain F against F, TM-score 1.00
  • Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • P54198 · AlphaFold monomer V2.0 prediction for protein hira (P54198) · a predicted model of the same protein · chain F against A, TM-score 0.52

Analyse

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