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Crystal structure of S-adenosylmethionine tRNA ribosyltransferase (TM0574) from Thermotoga maritima at 2.00 A resolution

Analyse Crystal structure of S-adenosylmethionine tRNA ribosyltransferase (TM0574) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VKY
Type
protein
Length
563 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Thermotoga maritima
Molecule
S-adenosylmethionine:tRNA ribosyltransferase-isomerase
EC
5.-.-.-
UniProt
Q9WZ44
Ligands
UNL
Pockets
6 · best druggability 0.59

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 28% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 5.-.-.-)protein28029% helix, 33% strandQ9WZ44
BS-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 5.-.-.-)protein28328% helix, 34% strandQ9WZ44

Ligands and binding sites

  • UNL · Unknown ligand · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.590.8820empty
22650.550.7731UNL
32640.550.7734UNL
4760.340.7512empty
5630.330.7612empty

Interfaces

1 interface between chains.

  • A–B · 517 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 1VKY · Crystal structure of S-adenosylmethionine tRNA ribosyltransferase (TM0574) from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WZ44 · AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA… · a predicted model of the same protein · chain B against A, TM-score 0.72

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