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Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (prma)

Analyse Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (prma) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NXC
Type
protein
Length
249 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosomal protein L11 methyltransferase
EC
2.1.1.-
UniProt
Q84BQ9
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosomal protein L11 methyltransferase (EC 2.1.1.-)protein24937% helix, 33% strandQ84BQ9

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.490.7728empty
21260.440.7616empty

Compared structures

  • 2NXC · Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q84BQ9 · AlphaFold monomer V2.0 prediction for ribosomal protein L11 methyltransferase (Q84BQ9) · a predicted model of the same protein · chain A against A, TM-score 0.78

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