6zbu

Crystal structure of an NCoR1BBD2-BCL6BTB chimera in complex with the NcoR1 BBD1 corepressor peptide

Method: X-RAY DIFFRACTION Dmax: 136.6 Å Quality: REASONABLE

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

Nuclear receptor corepressor 1,B-cell lymphoma 6 protein

Homo sapiens

UniProt O75376

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1733–1741 Chain B; UniProt 1733–1741 Chain C; UniProt 1340–1356 Chain D; UniProt 1340–1356 Chain E; UniProt 1733–1741 Chain F; UniProt 1733–1741 Chain G; UniProt 1340–1356 Chain H; UniProt 1340–1356 Chain I; UniProt 1733–1741 Chain J; UniProt 1733–1741 Chain K; UniProt 1340–1356 Chain L; UniProt 1340–1356 Not recorded SO4 SULFATE ION × 28 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;1.34M Ammonium sulfate 0.67%(v/v) MPD 0.1M HEPES/ Sodium hydroxide pH 7.5 Resolution 2.46 Å R-free 0.259

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.

24 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCOR1_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 3–11; UniProt 1733–1741 Author chain B; PDBConstruct 3–11; UniProt 1733–1741 Author chain E; PDBConstruct 3–11; UniProt 1733–1741 Author chain F; PDBConstruct 3–11; UniProt 1733–1741 Author chain I; PDBConstruct 3–11; UniProt 1733–1741 Author chain J; PDBConstruct 3–11; UniProt 1733–1741 Author chain C; PDBConstruct 1–17; UniProt 1340–1356 Author chain D; PDBConstruct 1–17; UniProt 1340–1356 Author chain G; PDBConstruct 1–17; UniProt 1340–1356 Author chain H; PDBConstruct 1–17; UniProt 1340–1356 Author chain K; PDBConstruct 1–17; UniProt 1340–1356 Author chain L; PDBConstruct 1–17; UniProt 1340–1356

Nuclear receptor corepressor 1,B-cell lymphoma 6 protein

Homo sapiens

UniProt P41182

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 6–129 Chain B; UniProt 6–129 Chain E; UniProt 6–129 Chain F; UniProt 6–129 Chain I; UniProt 6–129 Chain J; UniProt 6–129 Not recorded Nuclear receptor corepressor 1 × 6 (O75376) SO4 SULFATE ION × 28 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;1.34M Ammonium sulfate 0.67%(v/v) MPD 0.1M HEPES/ Sodium hydroxide pH 7.5 Resolution 2.46 Å R-free 0.259

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.

245 other PDB entries and 265 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCL6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–137; UniProt 6–129 Author chain B; PDBConstruct 14–137; UniProt 6–129 Author chain E; PDBConstruct 14–137; UniProt 6–129 Author chain F; PDBConstruct 14–137; UniProt 6–129 Author chain I; PDBConstruct 14–137; UniProt 6–129 Author chain J; PDBConstruct 14–137; UniProt 6–129

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 6zbu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6zbu
Deposition date deposition_date2020-06-09
Structure title titleCrystal structure of an NCoR1BBD2-BCL6BTB chimera in complex with the NcoR1 BBD1 corepressor peptide
Keywords keywordsBCL6, NCoR1., TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.33
Radius of gyration Rg (electron density) rg_electron38.51
Forward intensity I(0) i0180796000.00
Molecular weight molecular_weight104630.0 kDa
Excluded volume excluded_volume129420 ų
Envelope volume envelope_volume172410 ų
Hydration-shell volume shell_volume39387 ų
Envelope diameter envelope_diameter145.7
Shell Rg shell_rg41.34
Envelope Rg envelope_rg39.06
Shape Rg shape_rg38.52
Total Rg total_rg38.65
Total atoms total_atoms7276
Residues n_residues883
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 dmax136.6
Rg (real space) rg_real38.60
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.8080e+08
I(0) uncertainty (real space) i0_real_error2.9470e+06
Rg (reciprocal space) rg_reciprocal38.44
I(0) (reciprocal space) i0_reciprocal180800000.0000
Solution quality estimate total_estimate0.6036
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha85780000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.714; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.731; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)