› 2jnj

Solution NMR

Solution structure of the p8 TFIIH subunit

Released:
DOI: 10.2210/pdb2jnj/pdb
PDB entry 2jnj coloured by chain, ensemble of 10 models, front view.
PDB entry 2jnj coloured by chain, ensemble of 10 models, side view.
PDB entry 2jnj coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy.
Vitorino M, Coin F, Zlobinskaya O, Atkinson RA, Moras D, Egly JM, Poterszman A, Kieffer B
J Mol Biol 368 473-80 (2007)
PMID: 17350038

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General transcription factor IIH subunit 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 8.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6ZYL4 (Residues: 1-71; Coverage: 100%)
Gene names: C6orf175, GTF2H5, TTDA
Sequence domains: Transcription factor TFIIH complex subunit Tfb5
Structure domains: TFB5-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity.
Cleaver et al. (2009)
9 more

1 mention without citation

Small molecule-based targeting of TTD-A dimerization to control TFIIH transcriptional activity represents a potential strategy for anticancer therapy.
Gervais et al. (2018)