Research workbench

Human HMT1 hnrnp methyltransferase-like 3 (S. cerevisiae) protein

Analyse Human HMT1 hnrnp methyltransferase-like 3 (S. cerevisiae) protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FYT
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase 3
EC: 2.1.1.-
UniProt: O60678
Ligands: SAH
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 3 (EC 2.1.1.-)	protein	311	27% helix, 38% strand	O60678

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

2 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	235	0.76	0.90	40	SAH
2	57	0.54	0.88	15	empty

Compared structures

2FYT · Human HMT1 hnRNP methyltransferase-like 3 (S. cerevisiae) protein · the same entry in another collection · chain A against A, TM-score 1.00
O60678 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 3 (O60678) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O60678
Elsewhere: RCSB PDB 2FYT · PDBe 2FYT · UniProt O60678

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