4owx

Structural basis of SOSS1 in complex with a 12nt ssDNA

Method: X-RAY DIFFRACTION Dmax: 92.3 Å Quality: REASONABLE

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

Integrator complex subunit 3

Homo sapiens

UniProt Q68E01

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 A; UniProt 1–500 Not recorded ;DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') ; × 1 SOSS complex subunit B1 × 1 (Q9BQ15) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;16% PEG3350, 0.1M MES pH6.0, 0.1M ammonium formate Resolution 2.30 Å R-free 0.226

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT3_HUMAN
Isoform Q68E01-2
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–500; UniProt 1–500

SOSS complex subunit B1

Homo sapiens

UniProt Q9BQ15

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 1–211 Not recorded ;DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') ; × 1 Integrator complex subunit 3 × 1 (Q68E01) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;16% PEG3350, 0.1M MES pH6.0, 0.1M ammonium formate Resolution 2.30 Å R-free 0.226

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SOSB1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–211; UniProt 1–211

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 4owx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4owx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4owx
Deposition date deposition_date2014-02-04
Structure title titleStructural basis of SOSS1 in complex with a 12nt ssDNA
Keywords keywordsSOSS1 complex, DNA double-strand breaks, homologous recombination, ssDNA- binding protein, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.53
Radius of gyration Rg (electron density) rg_electron28.26
Forward intensity I(0) i073553800.00
Molecular weight molecular_weight67687.0 kDa
Excluded volume excluded_volume84967 ų
Envelope volume envelope_volume105310 ų
Hydration-shell volume shell_volume31429 ų
Envelope diameter envelope_diameter98.3
Shell Rg shell_rg35.11
Envelope Rg envelope_rg28.48
Shape Rg shape_rg28.23
Total Rg total_rg29.03
Total atoms total_atoms4735
Residues n_residues580
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 dmax92.3
Rg (real space) rg_real29.49
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real7.3550e+07
I(0) uncertainty (real space) i0_real_error9.4920e+05
Rg (reciprocal space) rg_reciprocal29.51
I(0) (reciprocal space) i0_reciprocal73550000.0000
Solution quality estimate total_estimate0.7300
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23180000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.994; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4owxB00
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)