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Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog

Analyse Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VFG
Type
protein + RNA
Length
765 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA (75-mer); Poly a polymerase
EC
2.7.7.19
UniProt
O66728
Ligands
APC
Pockets
20 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 57% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CRNA (75-mer)rna31——
DRNA (75-mer)rna34——
APoly a polymerase (EC 2.7.7.19)protein34256% helix, 11% strandO66728
BPoly a polymerase (EC 2.7.7.19)protein35858% helix, 10% strandO66728

Ligands and binding sites

  • APC · Diphosphomethylphosphonic acid adenosyl ester · ligand · 2 copies · chains A, D, B

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16580.730.8046APC
26360.710.7934empty
34770.660.7830empty
46330.640.7534empty
51850.630.8427empty

Interfaces

3 interfaces between chains.

  • D–B · 874 Ų buried · 19 hydrogen bonds · protein-nucleic
  • C–A · 464 Ų buried · 4 hydrogen bonds · protein-nucleic
  • A–B · 114 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1VFG · Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an… · the same entry in another collection · chain C against C, TM-score 1.00
  • O66728 · AlphaFold monomer V2.0 prediction for a-adding tRNA nucleotidyltransferase (O66728) · a predicted model of the same protein · chain A against A, TM-score 0.97

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