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Cryo-EM of a pretermination complex with ERF1 and ERF3

Analyse Cryo-EM of a pretermination complex with ERF1 and ERF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CRN
Type
protein
Length
851 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ERF3 in ribosome bound ERF1-ERF3-gdpnp complex; ERF1 in ribosome-bound ERF1-ERF3-gdpnp…
UniProt
P05453, P12385
Ligands
GNP
Pockets
11 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 21% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
PERF3 in ribosome bound ERF1-ERF3-gdpnp complexprotein43012% helix, 23% strandP05453
XERF1 in ribosome-bound ERF1-ERF3-gdpnp complexprotein42129% helix, 16% strandP12385

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains P

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110760.830.84124empty
28260.800.8389empty
32080.650.8324empty
43200.640.8038empty
51240.630.8725empty

Interfaces

1 interface between chains.

  • P–X · 1405 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 covalent (covalent ligand).

Compared structures

  • 4CRN · Cryo-EM of a pretermination complex with eRF1 and eRF3 · the same entry in another collection · chain P against P, TM-score 1.00
  • P12385 · AlphaFold monomer V2.0 prediction for eukaryotic peptide chain release factor subunit 1… · a predicted model of the same protein · chain X against A, TM-score 0.83
  • P05453 · AlphaFold monomer V2.0 prediction for eukaryotic peptide chain release factor GTP-binding… · a predicted model of the same protein · chain P against A, TM-score 0.81

Analyse

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