› 8qqe

X-ray diffraction
3.46Å resolution

Crystal structure of the complex between DMC1 and the PhePP domain of BRCA2

Released:
DOI: 10.2210/pdb8qqe/pdb
PDB entry 8qqe coloured by chain, front view.
PDB entry 8qqe coloured by chain, side view.
PDB entry 8qqe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces.
Miron S, Legrand P, Dupaigne P, van Rossum-Fikkert SE, Ristic D, Majeed A, Kanaar R, Zinn-Justin S, Zelensky AN
Nucleic Acids Res (2024)
PMID: 38828772

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-246056 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Meiotic recombination protein DMC1/LIM15 homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 37.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14565 (Residues: 2-340; Coverage: 100%)
Gene names: DMC1, DMC1H, LIM15
Sequence domains:
Breast cancer type 2 susceptibility protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 20 amino acids
Theoretical weight: 2.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli #1/H766
UniProt:
  • Canonical: P51587 (Residues: 2398-2417; Coverage: 1%)
Gene names: BRCA2, FACD, FANCD1

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: I432
Unit cell:
a: 234.383Å b: 234.383Å c: 234.383Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.248 0.261
Expression systems:
  • Escherichia coli
  • Escherichia coli #1/H766

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