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UniProt Q9Y294

Histone chaperone ASF1A (Q9Y294)

Histone chaperone ASF1A (UniProt Q9Y294): 25 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 47 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q9Y294
Protein
Histone chaperone ASF1A
Experimental structures
25
Predicted models
1
Ligands
2
Pockets
47 · 7 records with a druggable one

Structures

26 records of Q9Y294 in the MolNFT archive: 25 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1TEYNMR structure of human histone chaperone, ASF1Asolution nmrA——
1TEYNMR structure of human histone chaperone, ASF1Asolution nmrA——
2I32Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex…x-ray diffractionA, B——
2I32Structure of a human ASF1A-hira complex and insights into specificity of histone chaperone complex…x-ray diffractionA, B——
3AADStructure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone…x-ray diffractionB, D——
3AADStructure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone…x-ray diffractionB, D——
5C3ICrystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and…x-ray diffractionA, E, I, M, Q, U——
5C3ICrystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and…x-ray diffractionA, E, I, M, Q, U——
6F0FCrystal structure ASF1-ip2_sx-ray diffractionA——
6F0FCrystal structure ASF1-IP2_Sx-ray diffractionA——
6F0GCrystal structure ASF1-ip3x-ray diffractionA, BSO42 (best 0.57)
6F0GCrystal structure ASF1-IP3x-ray diffractionA, BSO4—
6F0HCrystal structure ASF1-ip4x-ray diffractionA, CSO43 (best 0.55)
6F0HCrystal structure ASF1-IP4x-ray diffractionA, CSO4—
6ZUFUrea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperonex-ray diffractionA, BSO41 (best 0.39)
6ZUFUrea-based foldamer inhibitor chimera C2 in complex with ASF1 histone chaperonex-ray diffractionA, BURL, SO4—
7LNYApo structure of the Histone chaperone ASF1A residues 1-155x-ray diffractionA, B, C, D, E, F, G—10 (best 0.81)
7LNYApo structure of the histone chaperone ASF1A residues 1-155x-ray diffractionA, B, C, D, E, F, G——
7LO0Structure of human ASF1A in complex with a TLK2 peptidex-ray diffractionA, B, C, D, E, F, G, H——
7V6QCrystal structure of snasp-ASF1A-H3.1-H4 complexx-ray diffractionA, E——
8BV1Peptide inhibitor P4 in complex with ASF1 histone chaperonex-ray diffractionA, B, C, D, E, F—9 (best 0.72)
8CJ1Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperonex-ray diffractionA, B, C, D, E, F, G, H—14 (best 0.75)
8CJ2Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperonex-ray diffractionA, B, C, DSO45 (best 0.76)
8CJ3Urea-based foldamer inhibitor c3u_7 chimera in complex with ASF1 histone chaperonex-ray diffractionA——
8Z50Crystal structure of the ASF1-H3T-H4 complexx-ray diffractionA—3 (best 0.52)
Q9Y294AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294)predictedA——

Ligands

  • SO4 · Sulfate ion · in 7 records
  • URL · [(2~{S})-2-azanyl-4-methyl-pentyl]carbamic acid · in 1 record

Experiment against prediction

Elsewhere

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