MolNFT v1 · #22759 · protein

Dimerization domain of ef-ts from T. thermophilus

1TFE · Elongation factor ts: “Dimerization domain of ef-ts from T. thermophilus”. X-ray diffraction. MolNFT v1 #22759 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor ts	protein	142	53% helix, 25% strand	P43895

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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P43895
Elsewhere: RCSB PDB 1TFE · PDBe 1TFE · UniProt P43895

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