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Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei

Analyse Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B4V
Type
protein
Length
437 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.8
Source
Trypanosoma brucei
Molecule
RNA editing complex protein MP57
UniProt
Q86MV5
Ligands
K
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · resolution 1.8 · 1 distinct chain · 47% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA editing complex protein MP57protein43747% helix, 15% strandQ86MV5

Ligands and binding sites

  • K · Potassium ion · metal · 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
16030.700.7952empty
2670.360.7818K

Modifications

Observed in the structure: 15 modified (engineered).

Compared structures

  • 2B4V · Structural basis for UTP specificity of RNA editing tutases from trypanosoma brucei · the same entry in another collection · chain A against A, TM-score 1.00
  • Q86MV5 · AlphaFold monomer V2.0 prediction for terminal uridylyltransferase 2 (Q86MV5) · a predicted model of the same protein · chain A against A, TM-score 1.00

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