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The crystal structure of the yeast arginine methyltransferase SFM1 complexed with sah

Analyse The crystal structure of the yeast arginine methyltransferase SFM1 complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H5E
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase SFM1
EC: 2.1.1.-
UniProt: Q12314
Ligands: SAH
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase SFM1 (EC 2.1.1.-)	protein	212	31% helix, 19% strand	Q12314

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	162	0.73	0.91	29	SAH

Compared structures

5H5E · The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAH · the same entry in another collection · chain A against A, TM-score 1.00
Q12314 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase SFM1 (Q12314) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q12314
Elsewhere: RCSB PDB 5H5E · PDBe 5H5E · UniProt Q12314

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