MolNFT v1 · #426807 · protein

AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-4 specific (P38827)

P38827: “AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-4 specific (P38827)”. 8 pockets (best druggability 0.68). MolNFT v1 #426807 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: P38827
Type: protein
Length: 1,080 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x0D671490EE06E75975e90D7F99F73B20BE618744
Molecule: Histone-lysine N-methyltransferase, H3 lysine-4 specific
UniProt: P38827
Pockets: 8 · best druggability 0.68

Structure

1 distinct chain · 27% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase, H3 lysine-4 specific	protein	1080	27% helix, 13% strand	P38827

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	473	0.68	0.79	48	empty
2	198	0.53	0.78	29	empty
3	128	0.49	0.79	21	empty
4	127	0.43	0.76	16	empty
5	73	0.32	0.74	20	empty

Compared structures

6VEN · Yeast compass in complex with a ubiquitinated nucleosome · an experimental structure of the same protein · chain A against N, TM-score 0.20
2J8A · X-ray structure of the N-terminus RRM domain of Set1 · an experimental structure of the same protein · chain A against A, TM-score 0.10
2J8A · X-ray structure of the N-terminus rrm domain of SET1 · an experimental structure of the same protein · chain A against A, TM-score 0.10

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 P38827
Elsewhere: UniProt P38827 · AlphaFold DB P38827

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