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Structure of the nosiheptide-resistance methyltransferase

Analyse Structure of the nosiheptide-resistance methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3NK6
Type
protein
Length
521 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
23S rRNA methyltransferase
EC
2.1.1.-
UniProt
P52391
Pockets
6 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A23S rRNA methyltransferase (EC 2.1.1.-)protein26439% helix, 20% strandP52391
B23S rRNA methyltransferase (EC 2.1.1.-)protein25739% helix, 21% strandP52391

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13110.660.8151empty
21110.640.8923empty
31200.420.7622empty
41200.420.7621empty
5900.420.7820empty

Interfaces

1 interface between chains.

  • A–B · 1279 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 3NK6 · Structure of the Nosiheptide-resistance methyltransferase · the same entry in another collection · chain B against B, TM-score 1.00
  • P52391 · AlphaFold monomer V2.0 prediction for 23S rRNA (ADENOSINE(1067)-2'-O)-methyltransferase… · a predicted model of the same protein · chain B against A, TM-score 0.98

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