X-ray diffraction
1.9Å resolution

Structure of human mitochondrial transcription elongation factor (TEFM) C-terminal domain


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Transcription elongation factor, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 319 amino acids
Theoretical weight: 37.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q96QE5 (Residues: 51-360; Coverage: 86%)
Gene names: C17orf42, TEFM
Sequence domains: Helix-hairpin-helix motif

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 98.48Å b: 112.54Å c: 88.84Å
α: 90° β: 110.13° γ: 90°
R R work R free
0.197 0.195 0.228
Expression system: Escherichia coli BL21(DE3)