8qqe

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

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Meiotic recombination protein DMC1/LIM15 homolog

Homo sapiens

UniProt Q14565

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 16 Breast cancer type 2 susceptibility protein × 8 (P51587) MAGNESIUM ION × 4 CHLORIDE ION × 8 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DMC1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–340; UniProt 2–340 Author chain B; PDBConstruct 2–340; UniProt 2–340

Breast cancer type 2 susceptibility protein

Homo sapiens

UniProt P51587

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 16 Meiotic recombination protein DMC1/LIM15 homolog × 8 (Q14565) MAGNESIUM ION × 4 CHLORIDE ION × 8 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BRCA2_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 2398–2417 Author chain D; PDBConstruct 1–20; UniProt 2398–2417

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qqe
Deposition date deposition_date2023-10-04
Structure title titleCrystal structure of the complex between DMC1 and the PhePP domain of BRCA2
Keywords keywordsDNA BINDING PROTEIN, Meiotic recombination, RING PROTEIN, OCTAMER, AAA ATPASE, RECOMBINATION; RECOMBINATION
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8qqe__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8qqe__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8qqe__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)48.18 Å
Rg (electron density)47.56 Å
Total Rg47.84 Å
Atom count17508
Residues2244
Excluded volume313140 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8qqe__assembly_1__model_1 hexadecameric (16) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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7. Citations (1)