1mje

STRUCTURE OF A BRCA2-DSS1-SSDNA COMPLEX

Method: X-RAY DIFFRACTION Dmax: 121.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Deleted in split hand/split foot protein 1

Homo sapiens

UniProt P60896

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–DNA Heteromer Protein × 2 DNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 1–70 Not recorded 5'-D(P*TP*TP*TP*TP*TP*T)-3' × 1 breast cancer 2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;277 K;Sodium Acetate, Sodium Citrate, NaCl, DTT, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.50 Å R-free 0.278

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.

124 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DSS1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–70; UniProt 1–70

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 1mje

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mje
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mje
Deposition date deposition_date2002-08-27
Structure title titleSTRUCTURE OF A BRCA2-DSS1-SSDNA COMPLEX
Keywords keywordsTUMOR SUPPRESSOR, BREAST CANCER SUSCEPTIBILITY, DNA-BINDING, GENE REGULATION-ANTITUMOR PROTEIN-DNA COMPLEX; GENE REGULATION/ANTITUMOR PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.71
Radius of gyration Rg (electron density) rg_electron36.15
Forward intensity I(0) i085301400.00
Molecular weight molecular_weight73815.0 kDa
Excluded volume excluded_volume92460 ų
Envelope volume envelope_volume125380 ų
Hydration-shell volume shell_volume31747 ų
Envelope diameter envelope_diameter128.9
Shell Rg shell_rg37.84
Envelope Rg envelope_rg36.77
Shape Rg shape_rg36.12
Total Rg total_rg36.36
Total atoms total_atoms5198
Residues n_residues648
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 dmax121.4
Rg (real space) rg_real36.20
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real8.5300e+07
I(0) uncertainty (real space) i0_real_error1.5710e+06
Rg (reciprocal space) rg_reciprocal35.90
I(0) (reciprocal space) i0_reciprocal85280000.0000
Solution quality estimate total_estimate0.7647
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.587
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18040000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.611; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.503; Smooth: 0.602

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1mjea1
Class classa — All alpha proteins
Fold Fold folda.170 — BRCA2 helical domain
Superfamily Superfamily superfamilya.170.1 — BRCA2 helical domain
Family Family familya.170.1.1 — BRCA2 helical domain
Domain ID domain_idd1mjea2
Class classa — All alpha proteins
Fold Fold folda.171 — BRCA2 tower domain
Superfamily Superfamily superfamilya.171.1 — BRCA2 tower domain
Family Family familya.171.1.1 — BRCA2 tower domain
Domain ID domain_idd1mjea3
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.3 — Single strand DNA-binding domain, SSB
Domain ID domain_idd1mjea4
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.3 — Single strand DNA-binding domain, SSB
Domain ID domain_idd1mjea5
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.3 — Single strand DNA-binding domain, SSB

CATH v4.4 (3 domains)

Domain ID domain_id1mjeA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id1mjeA03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id1mjeA04
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)