› 1koy

Solution NMR

NMR structure of DFF-C domain

Released:
DOI: 10.2210/pdb1koy/pdb
PDB entry 1koy coloured by chain, front view.
PDB entry 1koy coloured by chain, side view.
PDB entry 1koy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation.
Fukushima K, Kikuchi J, Koshiba S, Kigawa T, Kuroda Y, Yokoyama S
J Mol Biol 321 317-27 (2002)
PMID: 12144788

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA fragmentation factor subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 62 amino acids
Theoretical weight: 7.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00273 (Residues: 239-300; Coverage: 19%)
Gene names: DFF1, DFF45, DFFA, H13
Structure domains: C-terminal domain of DFF45/ICAD (DFF-C domain)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The protein structures that shape caspase activity, specificity, activation and inhibition.
Fuentes-Prior et al. (2004)
2 more

8 mentions without citation

Modification and optimization of the united-residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins.
Liwo et al. (2007)
7 more