8qqe

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

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: GOOD

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 2–340 Chain B; UniProt 2–340 Not recorded Breast cancer type 2 susceptibility protein × 8 (P51587) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;0.1M MES at pH 6, 2.4 M sodium formate Resolution 3.46 Å R-free 0.261

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain C; UniProt 2398–2417 Chain D; UniProt 2398–2417 Not recorded Meiotic recombination protein DMC1/LIM15 homolog × 8 (Q14565) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;0.1M MES at pH 6, 2.4 M sodium formate Resolution 3.46 Å R-free 0.261

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8qqe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qqe
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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

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.60
Radius of gyration Rg (electron density) rg_electron25.60
Forward intensity I(0) i062499800.00
Molecular weight molecular_weight62238.0 kDa
Excluded volume excluded_volume78286 ų
Envelope volume envelope_volume98605 ų
Hydration-shell volume shell_volume31600 ų
Envelope diameter envelope_diameter88.0
Shell Rg shell_rg33.39
Envelope Rg envelope_rg25.98
Shape Rg shape_rg25.59
Total Rg total_rg26.50
Total atoms total_atoms4377
Residues n_residues561
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax85.8
Rg (real space) rg_real26.53
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real6.2500e+07
I(0) uncertainty (real space) i0_real_error1.0040e+06
Rg (reciprocal space) rg_reciprocal26.55
I(0) (reciprocal space) i0_reciprocal62500000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.5
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12590000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)