GL1X · GenesisL1 explorer

MolNFT v1 · #181387 · protein

Structure of the alpha-N-methyltransferase (sonm mutant Y58F) and ripp precursor (sona) heteromeric complex (no cofactor)

7LTF · Tp-methylase family protein: “Structure of the alpha-N-methyltransferase (sonm mutant Y58F) and ripp precursor (sona) heteromeric complex…”. X-ray diffraction, 8 pockets (best druggability 0.70). MolNFT v1 #181387 on GenesisL1: 3D…

PDB
7LTF
Type
protein
Length
661 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tp-methylase family protein; Liga domain-containing protein
UniProt
Q8EGW3, Q8EGW2
Pockets
8 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CTp-methylase family proteinprotein26237% helix, 21% strandQ8EGW3
BLiga domain-containing proteinprotein6961% helix, 1% strandQ8EGW2
DLiga domain-containing proteinprotein6860% helix, 1% strandQ8EGW2

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.700.9820empty
2510.700.9819empty
32730.640.8137empty
42480.630.8134empty
52910.580.7747empty

Interfaces

5 interfaces between chains.

  • A–C · 2859 Ų buried · 54 hydrogen bonds · protein-protein
  • C–D · 1720 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 1670 Ų buried · 21 hydrogen bonds · protein-protein
  • A–D · 513 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 502 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

  • 7LTF · Structure of the alpha-N-methyltransferase (SonM mutant Y58F) and RiPP precursor (SonA)… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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