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Crystal structure of peptidyl-tRNA hydrolase from escherichia COLI in complex with the cca-acceptor-T[PSI]C domain of tRNA

Analyse Crystal structure of peptidyl-tRNA hydrolase from escherichia COLI in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VJR
Type
protein + RNA
Length
458 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-tRNA hydrolase; TRNA cca-acceptor
EC
3.1.1.29
UniProt
P0A7D1
Pockets
8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CPeptidyl-tRNA hydrolase (EC 3.1.1.29)protein19344% helix, 21% strandP0A7D1
B, DTRNA cca-acceptorrna36——

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15940.760.8349empty
23730.700.8326empty
32440.660.8436empty
42780.630.8139empty
5550.260.7315empty

Interfaces

6 interfaces between chains.

  • C–D · 706 Ų buried · 12 hydrogen bonds · protein-nucleic
  • A–B · 695 Ų buried · 15 hydrogen bonds · protein-nucleic
  • B–D · 566 Ų buried · 39 hydrogen bonds · nucleic-nucleic
  • A–D · 38 Ų buried · 1 hydrogen bond · protein-nucleic
  • B–C · 36 Ų buried · 1 hydrogen bond · protein-nucleic

Compared structures

  • 3VJR · Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A7D1 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (P0A7D1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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