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

Analyse Structure of the alpha-N-methyltransferase (sonm) and ripp precursor (sona)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LTC
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 0.71

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
1530.710.9820empty
2500.680.9719empty
32640.640.8136empty
42490.630.8136empty
52390.560.7834empty

Interfaces

5 interfaces between chains.

  • A–C · 2850 Ų buried · 53 hydrogen bonds · protein-protein
  • C–D · 1726 Ų buried · 25 hydrogen bonds · protein-protein
  • A–B · 1664 Ų buried · 25 hydrogen bonds · protein-protein
  • A–D · 508 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 499 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

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

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