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UniProt Q12692

Histone H2A.Z (Q12692)

Histone H2A.Z (UniProt Q12692): 6 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q12692
Protein
Histone H2A.Z
Experimental structures
6
Predicted models
1
Ligands
1

Structures

7 records of Q12692 in the MolNFT archive: 6 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
2JSSNMR structure of chaperone Chz1 complexed with histone H2A.Z-H2Bsolution nmrA——
2JSSNMR structure of chaperone CHZ1 complexed with histone H2A.Z-H2Bsolution nmrA——
4M6BCrystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimerx-ray diffractionA, D——
4M6BCrystal structure of yeast SWR1-Z domain in complex with H2A.Z-H2B dimerx-ray diffractionA, D——
6AE8Structure insight into histone chaperone CHZ1-mediated H2A.Z recognition and replacementx-ray diffractionA, BBCN—
8QZ0SWR1-hexasome-dimer complexelectron microscopyL——
Q12692AlphaFold monomer V2.0 prediction for histone H2A.Z (Q12692)predictedA——

Ligands

  • BCN · Bicine · in 1 record

Experiment against prediction

Elsewhere

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