› 5gow

Solution NMR

Solution structure of the complex between DP1 acidic region and TFIIH p62 PH domain

Released:
DOI: 10.2210/pdb5gow/pdb
PDB 5gow coloured by chain and viewed from the front.
PDB 5gow coloured by chain and viewed from the side.
PDB 5gow coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
The Interaction Mode of the Acidic Region of the Cell Cycle Transcription Factor DP1 with TFIIH.
Okuda M, Araki K, Ohtani K, Nishimura Y
J. Mol. Biol. (2016)
PMID: 27825926

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription factor Dp-1 Chain: A
Molecule details ›
Chain: A
Length: 19 amino acids
Theoretical weight: 2.28 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q14186 (Residues: 392-410; Coverage: 5%)
Gene names: DP1, TFDP1
General transcription factor IIH subunit 1 Chain: B
Molecule details ›
Chain: B
Length: 110 amino acids
Theoretical weight: 12.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32780 (Residues: 1-108; Coverage: 20%)
Gene names: BTF2, GTF2H1
Sequence domains: TFIIH p62 subunit, N-terminal domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: DGSA-distance geometry simulated annealing
Chemical shifts: BMR36013  
Expression systems:
  • Not provided
  • Escherichia coli

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Citations

3 citation in other articles

Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.
Okuda et al. (2017)
2 more