6qnx

Structure of the SA2/SCC1/CTCF complex

Method: X-RAY DIFFRACTION Dmax: 132.8 Å Quality: GOOD

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

Cohesin subunit SA-2

Homo sapiens

UniProt Q8N3U4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 80–1060 Not recorded 64-kDa C-terminal product × 1 (O60216) Transcriptional repressor CTCF × 1 (P49711) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.06M Morpheus Divalents mix, 0.1M Morpheus buffer system 1, 48% (v/v) Morpheus EOD_P8K Resolution 2.70 Å

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.

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

View Construct and Data Evidence
UniProt name STAG2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–981; UniProt 80–1060

64-kDa C-terminal product

Homo sapiens

UniProt O60216

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 281–420 Not recorded Cohesin subunit SA-2 × 1 (Q8N3U4) Transcriptional repressor CTCF × 1 (P49711) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.06M Morpheus Divalents mix, 0.1M Morpheus buffer system 1, 48% (v/v) Morpheus EOD_P8K Resolution 2.70 Å

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.

35 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD21_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–140; UniProt 281–420

Transcriptional repressor CTCF

OrganismNot specified

UniProt P49711

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 222–231 Not recorded Cohesin subunit SA-2 × 1 (Q8N3U4) 64-kDa C-terminal product × 1 (O60216) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.06M Morpheus Divalents mix, 0.1M Morpheus buffer system 1, 48% (v/v) Morpheus EOD_P8K Resolution 2.70 Å

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.

20 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTCF_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 222–231

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 6qnx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qnx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qnx
Deposition date deposition_date2019-02-12
Structure title titleStructure of the SA2/SCC1/CTCF complex
Keywords keywordsCohesin, CTCF, TAD, Chromatin folding, genome regulation, SA2, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.78
Radius of gyration Rg (electron density) rg_electron39.17
Forward intensity I(0) i0201092000.00
Molecular weight molecular_weight117170.0 kDa
Excluded volume excluded_volume147550 ų
Envelope volume envelope_volume206950 ų
Hydration-shell volume shell_volume44372 ų
Envelope diameter envelope_diameter137.5
Shell Rg shell_rg44.70
Envelope Rg envelope_rg38.44
Shape Rg shape_rg39.17
Total Rg total_rg39.52
Total atoms total_atoms16463
Residues n_residues1011
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 dmax132.8
Rg (real space) rg_real39.83
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real2.0110e+08
I(0) uncertainty (real space) i0_real_error3.4620e+06
Rg (reciprocal space) rg_reciprocal39.81
I(0) (reciprocal space) i0_reciprocal201100000.0000
Solution quality estimate total_estimate0.8835
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.8
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.580
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21970000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.842

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)