2kz3

Solution NMR

Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83

Released:
Source organism: Homo sapiens
Primary publication:
Structural and functional characterization of the N-terminal domain of human Rad51D.
Int J Biochem Cell Biol 43 416-22 (2011)
PMID: 21111057

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein RAD51 homolog 4 Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75771 (Residues: 1-83; Coverage: 25%)
Gene names: RAD51D, RAD51L3
Sequence domains: RAD51D, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli