8ssr

ZnFs 3-11 of CCCTC-binding factor (CTCF) Complexed with 35mer DNA 35-20

Method: X-RAY DIFFRACTION Dmax: 140.9 Å Quality: GOOD

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

Transcriptional repressor CTCF

Homo sapiens

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 319–606 Fragment:Zinc finger domains 3-11 DNA (35-MER) Strand I × 1 DNA (35-MER) Strand II × 1 ZN ZINC ION × 9 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;20-25%% w/v PEG 3,350, 0.1 M BIS-TRIS pH 5.0-6.5, 0.05-0.20M NaCl Resolution 3.14 Å R-free 0.284
2 Protein–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain D; UniProt 319–606 Fragment:Zinc finger domains 3-11 DNA (35-MER) Strand I × 1 DNA (35-MER) Strand II × 1 ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;20-25%% w/v PEG 3,350, 0.1 M BIS-TRIS pH 5.0-6.5, 0.05-0.20M NaCl Resolution 3.14 Å R-free 0.284

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 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTCF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–288; UniProt 319–606 Author chain D; PDBConstruct 1–288; UniProt 319–606

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 8ssr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ssr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ssr
Deposition date deposition_date2023-05-08
Structure title titleZnFs 3-11 of CCCTC-binding factor (CTCF) Complexed with 35mer DNA 35-20
Keywords keywords;PROTEIN-DNA COMPLEX, DNA BINDING PROTEIN, transcription factor, zinc fingers, insulator/chromatin architecture, transcription-dna complex, TRANSCRIPTION ;; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.68
Radius of gyration Rg (electron density) rg_electron40.92
Forward intensity I(0) i0283217000.00
Molecular weight molecular_weight102370.0 kDa
Excluded volume excluded_volume113290 ų
Envelope volume envelope_volume187770 ų
Hydration-shell volume shell_volume41333 ų
Envelope diameter envelope_diameter149.5
Shell Rg shell_rg43.18
Envelope Rg envelope_rg39.77
Shape Rg shape_rg40.90
Total Rg total_rg41.06
Total atoms total_atoms6926
Residues n_residues630
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 dmax140.9
Rg (real space) rg_real40.91
Rg uncertainty (real space) rg_real_error1.62
I(0) (real space) i0_real2.8320e+08
I(0) uncertainty (real space) i0_real_error5.4600e+06
Rg (reciprocal space) rg_reciprocal40.68
I(0) (reciprocal space) i0_reciprocal283100000.0000
Solution quality estimate total_estimate0.8590
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.4
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.253
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7323000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.827; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)