› 1nha

Solution NMR

Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF

Released:
DOI: 10.2210/pdb1nha/pdb
PDB entry 1nha coloured by chain, ensemble of 20 models, front view.
PDB entry 1nha coloured by chain, ensemble of 20 models, side view.
PDB entry 1nha coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG
Biochemistry 42 1460-9 (2003)
PMID: 12578358

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General transcription factor IIF subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35269 (Residues: 436-517; Coverage: 16%)
Gene names: GTF2F1, RAP74
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The general transcription machinery and general cofactors.
Thomas et al. (2006)
3 more

4 mentions without citation

Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators.
De Mol et al. (2018)
3 more