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DOT1L structure in complex with sah

Analyse DOT1L structure in complex with sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QOX
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase
EC: 2.1.1.43
UniProt: Q8TEK3
Ligands: SAH, SO4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase (EC 2.1.1.43)	protein	326	42% helix, 14% strand	Q8TEK3

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	337	0.68	0.81	55	SAH
2	149	0.48	0.77	24	empty
3	99	0.37	0.75	15	empty

Compared structures

3QOX · DOT1L structure in complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
Q8TEK3 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-79… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8TEK3
Elsewhere: RCSB PDB 3QOX · PDBe 3QOX · UniProt Q8TEK3

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