Research workbench

AlphaFold monomer V2.0 prediction for 2-ketoarginine methyltransferase (D5FKJ3)

Analyse AlphaFold monomer V2.0 prediction for 2-ketoarginine methyltransferase (D5FKJ3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: D5FKJ3
Type: protein
Length: 350 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x4a689cCb8B548104f45568fF88692AEd958A42D9
Molecule: 2-ketoarginine methyltransferase
UniProt: D5FKJ3
Pockets: 3 · best druggability 0.75

Structure

1 distinct chain · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-ketoarginine methyltransferase	protein	350	53% helix, 15% strand	D5FKJ3

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	391	0.75	0.85	55	empty
2	200	0.49	0.75	29	empty
3	88	0.31	0.72	19	empty

Compared structures

8R4Z · Crystal structure of alpha keto acid C-methyl-transferases MrsA native-form · an experimental structure of the same protein · chain A against A, TM-score 0.95
8RWM · Crystal structure of selenomethionine derivatized alpha keto acid C-methyl-transferases… · an experimental structure of the same protein · chain A against B, TM-score 0.95
8RVC · Crystal structure of alpha keto acid C-methyl-transferases MrsA bound to ketoarginine · an experimental structure of the same protein · chain A against B, TM-score 0.95

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 D5FKJ3
Elsewhere: UniProt D5FKJ3 · AlphaFold DB D5FKJ3

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