MolNFT v1 · #191458 · protein

Crystal structure of apo protein arginine N-methyltransferase 1 (PRMT1) from naegleria fowleri

8DUR: “Crystal structure of apo protein arginine N-methyltransferase 1 (PRMT1) from naegleria fowleri”. X-ray diffraction, 4 pockets (best druggability 0.61). MolNFT v1 #191458 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8DUR
Type: protein
Length: 634 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase 1 (PRMT1)
UniProt: A0A6A5BBK9
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 1 (PRMT1)	protein	314	28% helix, 39% strand	A0A6A5BBK9
B	Protein arginine N-methyltransferase 1 (PRMT1)	protein	320	27% helix, 38% strand	A0A6A5BBK9

Pockets

4 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	297	0.61	0.79	35	empty
2	308	0.60	0.78	32	empty
3	117	0.47	0.79	19	empty
4	129	0.46	0.77	18	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

8DUR · Crystal structure of apo protein arginine N-methyltransferase 1 (PRMT1) from Naegleria… · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A6A5BBK9
Elsewhere: RCSB PDB 8DUR · PDBe 8DUR · UniProt A0A6A5BBK9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.