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UniProt Q16695

Histone H3.1t peptide (Q16695)

Histone H3.1t peptide (UniProt Q16695): 22 experimental structures on GenesisL1, 1 ligand bound, 9 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q16695
Protein
Histone H3.1t peptide
Experimental structures
22
Predicted models
0
Ligands
1
Pockets
9 · 3 records with a druggable one

Structures

22 records of Q16695 in the MolNFT archive: 22 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2V1DStructural basis of LSD1-CoREST selectivity in histone H3 recognitionx-ray diffractionC——
2V1DStructural basis of LSD1-corest selectivity in histone H3 recognitionx-ray diffractionC——
2YBPJMJD2A COMPLEXED WITH R-2-HYDROXYGLUTARATE AND HISTONE H3K36me3 PEPTIDE (30-41)x-ray diffractionC, D——
2YBPJMJD2A complexed with R-2-hydroxyglutarate and histone H3K36ME3 peptide (30-41)x-ray diffractionC, D——
2YBSJMJD2A COMPLEXED WITH S-2-HYDROXYGLUTARATE AND HISTONE H3K36me3 PEPTIDE (30-41)x-ray diffractionC, D——
2YBSJMJD2A complexed with S-2-hydroxyglutarate and histone H3K36ME3 peptide (30-41)x-ray diffractionC, D——
3A6NThe nucleosome containing a testis-specific histone variant, human H3Tx-ray diffractionA, E——
3A6NThe nucleosome containing a testis-specific histone variant, human H3Tx-ray diffractionA, E——
3T6RStructure of UHRF1 in complex with unmodified H3 N-terminal tailx-ray diffractionD——
3T6RStructure of UHRF1 in complex with unmodified H3 N-terminal tailx-ray diffractionD——
4A7JSymmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin…x-ray diffractionB——
4A7JSymmetric dimethylation of H3 arginine 2 is a novel histone mark that supports euchromatin…x-ray diffractionB——
4V2VJMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H3K27me3 PEPTIDE (25-29) ARK(me3)SAx-ray diffractionC, D——
4V2VJMJD2A complexed with NI(II), nog and histone H3K27ME3 peptide (25-29) ARK(ME3)SAx-ray diffractionC, D——
4V2WJMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H3K27me3 PEPTIDE (16-35)x-ray diffractionC——
4V2WJMJD2A complexed with NI(II), nog and histone H3K27ME3 peptide (16-35)x-ray diffractionC——
6OIEThe double PHD finger (DPF) of MORF in complex with histone H3K14crx-ray diffractionC, D—1 (best 0.60)
6OIEThe double phd finger (dpf) of morf in complex with histone H3K14CRx-ray diffractionC, D——
6WATcomplex structure of PHF1x-ray diffractionA, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, V, Y, Z, a, b, c, d, e, f, gUNX6 (best 0.52)
6WAUComplex structure of PHF19x-ray diffractionG, H, I, J, K, L——
8Z50Crystal structure of the ASF1-H3T-H4 complexx-ray diffractionB—2 (best 0.52)
Q16695AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695)———

Ligands

  • UNX · Unknown atom or ion · in 1 record

Elsewhere

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