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UniProt Q53H47

Histone-lysine N-methyltransferase SETMAR (Q53H47)

Histone-lysine N-methyltransferase SETMAR (UniProt Q53H47), EC 2.1.1.357, 3.1.-.-: 11 experimental structures on GenesisL1, 1 pocket. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q53H47
Protein
Histone-lysine N-methyltransferase SETMAR
EC
2.1.1.357, 3.1.-.-
Experimental structures
11
Predicted models
0
Pockets
1 · 0 records with a druggable one

Structures

11 records of Q53H47 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
3BO5Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMARx-ray diffractionA——
3BO5Crystal structure of methyltransferase domain of human histone-lysine N-methyltransferase setmarx-ray diffractionA——
3F2KStructure of the transposase domain of human Histone-lysine N-methyltransferase SETMARx-ray diffractionA, B——
3F2KStructure of the transposase domain of human histone-lysine N-methyltransferase setmarx-ray diffractionA, B——
3K9JTransposase domain of Metnasex-ray diffractionA, B——
3K9JTransposase domain of metnasex-ray diffractionA, B——
3K9KTransposase domain of Metnasex-ray diffractionA, B——
3K9KTransposase domain of metnasex-ray diffractionA, B——
7S03DNA-binding domain of human SETMAR in complex with Hsmar1 terminal inverted repeat (TIR) DNAx-ray diffractionA—1 (best 0.42)
7S03DNA-binding domain of human setmar in complex with HSMAR1 terminal inverted repeat (tir) DNAx-ray diffractionA——
Q53H47AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase setmar (Q53H47)———

Elsewhere

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