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Crystal structure of ribosomal protein L11 methyltransferase from thermus thermophilus in complex with S-adenosyl-L-homocysteine

Analyse Crystal structure of ribosomal protein L11 methyltransferase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZBQ
Type
protein
Length
251 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
Ligands
SAH
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosomal protein L11 methyltransferase (EC 2.1.1.-)protein25133% helix, 32% strandQ84BQ9

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12130.510.7732SAH
21180.460.7818empty

Compared structures

  • 2ZBQ · Crystal structure of ribosomal protein L11 methyltransferase from Thermus thermophilus in… · 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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