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Structure of the alpha-N-methyltransferase (sonm mutant Y93F) and ripp precursor (sona) heteromeric complex (no cofactor)

Analyse Structure of the alpha-N-methyltransferase (sonm mutant Y93F) and ripp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LTH
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 0.77

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, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.770.9723empty
2940.760.9725empty
32560.650.8237empty
42550.630.8136empty
52560.550.7736empty

Interfaces

5 interfaces between chains.

  • A–C · 2853 Ų buried · 54 hydrogen bonds · protein-protein
  • A–B · 1701 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1694 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 521 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 504 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

  • 7LTH · Structure of the alpha-N-methyltransferase (SonM mutant Y93F) and RiPP precursor (SonA)… · the same entry in another collection · chain A against A, TM-score 1.00

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