› 2lyh

Solution NMR

Structure of Faap24 residues 141-215

Released:
DOI: 10.2210/pdb2lyh/pdb
PDB entry 2lyh coloured by chain, ensemble of 20 models, front view.
PDB entry 2lyh coloured by chain, ensemble of 20 models, side view.
PDB entry 2lyh coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition.
Wienk H, Slootweg JC, Speerstra S, Kaptein R, Boelens R, Folkers GE
Nucleic Acids Res 41 6739-49 (2013)
PMID: 23661679

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fanconi anemia core complex-associated protein 24 Chain: A
Molecule details ›
Chain: A
Length: 98 amino acids
Theoretical weight: 10.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BTP7 (Residues: 139-215; Coverage: 36%)
Gene names: C19orf40, FAAP24
Sequence domains: Helix-hairpin-helix motif
Structure domains: 5' to 3' exonuclease, C-terminal subdomain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Function and Interactions of ERCC1-XPF in DNA Damage Response.
Faridounnia et al. (2018)
2 other articles

3 mentions without citation

Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response.
Wang et al. (2013)
2 more