› 5g32

X-ray diffraction
2.2Å resolution

Structure of Rad14 in complex with acetylaminophenyl-guanine containing DNA

Released:
DOI: 10.2210/pdb5g32/pdb
PDB entry 5g32 coloured by chain, front view.
PDB entry 5g32 coloured by chain, side view.
PDB entry 5g32 coloured by chain, top view.
Source organisms:
Primary publication:
Structural Basis for Bulky-Adduct DNA-Lesion Recognition by the Nucleotide Excision Repair Protein Rad14.
Simon N, Ebert C, Schneider S
Chemistry 22 10782-5 (2016)
PMID: 27223336

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-118695 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA repair protein RAD14 Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.61 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P28519 (Residues: 188-306; Coverage: 32%)
Gene names: RAD14, YM8325.02C, YMR201C
Sequence domains: XPA protein C-terminus
5'-D(*GP*CP*TP*CP*TP*AP*6FKP*TP*CP*AP*TP*CP*AP*CP)-3' Chains: C, E
Molecule details ›
Chains: C, E
Length: 15 nucleotides
Theoretical weight: 4.64 KDa
Source organism: synthetic construct
5'-D(*GP*TP*GP*AP*TP*GP*AP*CP*GP*TP*AP*GP*AP*GP)-3' Chains: D, F
Molecule details ›
Chains: D, F
Length: 14 nucleotides
Theoretical weight: 4.38 KDa
Source organism: synthetic construct

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand 6FK 2 x 6FK

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P41
Unit cell:
a: 52.964Å b: 52.964Å c: 130.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.266
Expression system: Escherichia coli BL21

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Citations

1 review citation

The XPA Protein-Life under Precise Control.
Krasikova et al. (2022)
5 other articles