6py8

Crystal structure of the RBPJ-NOTCH1-NRARP ternary complex bound to DNA

Method: X-RAY DIFFRACTION Dmax: 143.1 Å Quality: GOOD

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

Notch-regulated ankyrin repeat-containing protein

Homo sapiens

UniProt Q7Z6K4

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 × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain B; UniProt 1–114 Not recorded DNA × 1 DNA × 1 Recombining binding protein suppressor of hairless × 1 (Q06330) Neurogenic locus notch homolog protein 1 × 1 (P46531) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315
2 Protein–DNA Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain G; UniProt 1–114 Not recorded DNA × 1 DNA × 1 Recombining binding protein suppressor of hairless × 1 (Q06330) Neurogenic locus notch homolog protein 1 × 1 (P46531) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name NRARP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–114; UniProt 1–114 Author chain G; PDBConstruct 1–114; UniProt 1–114

Recombining binding protein suppressor of hairless

Homo sapiens

UniProt Q06330

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 × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain E; UniProt 23–466 Not recorded Notch-regulated ankyrin repeat-containing protein × 1 (Q7Z6K4) DNA × 1 DNA × 1 Neurogenic locus notch homolog protein 1 × 1 (P46531) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315
2 Protein–DNA Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain C; UniProt 23–466 Not recorded Notch-regulated ankyrin repeat-containing protein × 1 (Q7Z6K4) DNA × 1 DNA × 1 Neurogenic locus notch homolog protein 1 × 1 (P46531) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUH_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–444; UniProt 23–466 Author chain E; PDBConstruct 1–444; UniProt 23–466

Neurogenic locus notch homolog protein 1

Homo sapiens

UniProt P46531

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 × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain F; UniProt 1759–2127 Not recorded Notch-regulated ankyrin repeat-containing protein × 1 (Q7Z6K4) DNA × 1 DNA × 1 Recombining binding protein suppressor of hairless × 1 (Q06330) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315
2 Protein–DNA Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain K; UniProt 1759–2127 Not recorded Notch-regulated ankyrin repeat-containing protein × 1 (Q7Z6K4) DNA × 1 DNA × 1 Recombining binding protein suppressor of hairless × 1 (Q06330) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;50 mM Hepes pH 6.8, 200 mM Sodium Fluoride, 18% PEG 3350 Resolution 3.75 Å R-free 0.315

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.

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

View Construct and Data Evidence
UniProt name NOTC1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–369; UniProt 1759–2127 Author chain K; PDBConstruct 1–369; UniProt 1759–2127

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 6py8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6py8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6py8
Deposition date deposition_date2019-07-29
Structure title titleCrystal structure of the RBPJ-NOTCH1-NRARP ternary complex bound to DNA
Keywords keywordsNOTCH1, NRARP, RBPJ, DNA 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_guinier44.78
Radius of gyration Rg (electron density) rg_electron43.82
Forward intensity I(0) i0635106000.00
Molecular weight molecular_weight190340.0 kDa
Excluded volume excluded_volume231020 ų
Envelope volume envelope_volume349550 ų
Hydration-shell volume shell_volume65537 ų
Envelope diameter envelope_diameter154.5
Shell Rg shell_rg49.64
Envelope Rg envelope_rg43.23
Shape Rg shape_rg43.80
Total Rg total_rg44.12
Total atoms total_atoms13305
Residues n_residues1615
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 dmax143.1
Rg (real space) rg_real44.65
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real6.3510e+08
I(0) uncertainty (real space) i0_real_error1.2250e+07
Rg (reciprocal space) rg_reciprocal44.77
I(0) (reciprocal space) i0_reciprocal635200000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.164
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35960000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.768

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6py8C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1450 — LAG1, DNA binding domain
Domain ID domain_id6py8C02
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id6py8C03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6py8E01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1450 — LAG1, DNA binding domain
Domain ID domain_id6py8E02
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id6py8E03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6py8F00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id6py8K00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (1)

9. Files and Curves (10)