› 4dfc

X-ray diffraction
2.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141272 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription-repair-coupling factor Chains: A, C
Molecule details ›
Chains: A, C
Length: 93 amino acids
Theoretical weight: 10.58 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P30958 (Residues: 127-213; Coverage: 8%)
Gene names: JW1100, b1114, mfd
Sequence domains: UvrB interaction domain
Structure domains: Penicillin-binding protein 1b domain
UvrABC system protein A Chains: B, D
Molecule details ›
Chains: B, D
Length: 126 amino acids
Theoretical weight: 13.96 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A698 (Residues: 131-250; Coverage: 13%)
Gene names: JW4019, b4058, dinE, uvrA
Sequence domains: UvrA interaction domain
Structure domains: Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P6222
Unit cell:
a: 119.168Å b: 119.168Å c: 234.334Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.238 0.282
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic nucleotide excision repair.
Kisker et al. (2013)
10 more

4 mentions without citation

From Mfd to TRCF and Back Again-A Perspective on Bacterial Transcription-coupled Nucleotide Excision Repair.
Deaconescu et al. (2017)
3 more