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Polypeptide chain release factor 2 (RF2) from escherichia COLI

Analyse Polypeptide chain release factor 2 (RF2) from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GQE
Type
protein
Length
362 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Release factor 2
UniProt
P07012
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARelease factor 2protein36251% helix, 21% strandP07012

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13480.630.7928empty
22320.510.7634empty
3750.420.8017empty
4840.360.7618empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 1GQE · Polypeptide Chain Release Factor 2 (RF2) from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P07012 · AlphaFold monomer V2.0 prediction for peptide chain release factor RF2 (P07012) · a predicted model of the same protein · chain A against A, TM-score 0.50

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