GL1X · GenesisL1 explorer

Research workbench

Cryo-EM structure of the apo form of human PRMT5:MEP50 complex at a resolution of 3.4 ångström

Analyse Cryo-EM structure of the apo form of human PRMT5:MEP50 complex at a resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6UGH
Type
protein
Length
895 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 5; Methylosome protein 50
EC
2.1.1.320
UniProt
O14744, Q9BQA1
Pockets
5 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 21% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 5 (EC 2.1.1.320)protein59431% helix, 25% strandO14744
BMethylosome protein 50protein3011% helix, 48% strandQ9BQA1

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110060.820.8476empty
26530.790.8467empty
32390.560.7826empty
42410.520.7523empty
52070.490.7631empty

Interfaces

1 interface between chains.

  • A–B · 2148 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 6UGH · Cryo-EM structure of the apo form of human PRMT5:MEP50 complex at a resolution of 3.4… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9BQA1 · AlphaFold monomer V2.0 prediction for methylosome protein 50 (Q9BQA1) · a predicted model of the same protein · chain B against A, TM-score 0.99
  • O14744 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 5 (O14744) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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