1f3u

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF

Released:
Source organism: Homo sapiens
Primary publication:
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.
J Mol Biol 302 1119-27 (2000)
PMID: 11183778

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-146829 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
General transcription factor IIF subunit 2 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 118 amino acids
Theoretical weight: 12.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13984 (Residues: 2-119; Coverage: 47%)
Gene names: GTF2F2, RAP30
Sequence domains: TFIIF, beta subunit N-terminus
General transcription factor IIF subunit 1 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 171 amino acids
Theoretical weight: 19.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35269 (Residues: 2-172; Coverage: 33%)
Gene names: GTF2F1, RAP74
Sequence domains: Transcription initiation factor IIF, alpha subunit (TFIIF-alpha)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 48.015Å b: 72.29Å c: 82.266Å
α: 104.51° β: 93.32° γ: 104.32°
R-values:
R R work R free
0.225 0.225 0.26
Expression system: Escherichia coli