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Dimerization domain of ef-ts from T. thermophilus

Analyse Dimerization domain of ef-ts from T. thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TFE
Type
protein
Length
142 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor ts
UniProt
P43895

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor tsprotein14253% helix, 25% strandP43895

Compared structures

  • 1TFE · Dimerization domain of ef-ts from T. thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
  • P43895 · AlphaFold monomer V2.0 prediction for elongation factor ts (P43895) · a predicted model of the same protein · chain A against A, TM-score 0.98

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