› 2n23

Solution NMR

NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the N-terminal activation domain of EKLF (TAD1)

Released:
DOI: 10.2210/pdb2n23/pdb
PDB entry 2n23 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n23 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n23 coloured by chain, ensemble of 20 models, top view.
Source organisms:
Entry authors: Lecoq L, Morse T, Raiola L, Arseneault G, Omichinski J

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-152447 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
General transcription and DNA repair factor IIH subunit TFB1 Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 12.9 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32776 (Residues: 2-115; Coverage: 18%)
Gene names: D9740.3, TFB1, YDR311W
Sequence domains: TFIIH p62 subunit, N-terminal domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Krueppel-like factor 1 Chain: B
Molecule details ›
Chain: B
Length: 19 amino acids
Theoretical weight: 2.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13351 (Residues: 22-40; Coverage: 5%)
Gene names: EKLF, KLF1
Sequence domains: Erythroid krueppel-like transcription factor, transactivation 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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