9b3g

Human Notch-1 EGFs 21-23

Method: X-RAY DIFFRACTION Dmax: 86.7 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 790–906 Fragment:Human Notch1 EGF domains 21-23 BA BARIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.2 M Ammonium acetate 0.1 M BIS-Tris pH 5.5 25% (w/v) PEG3350 Resolution 1.55 Å R-free 0.218

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 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NOTC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–119; UniProt 790–906

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 9b3g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b3g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b3g
Deposition date deposition_date2024-03-19
Structure title titleHuman Notch-1 EGFs 21-23
Keywords keywordsNotch, EGF, Calcium-binding, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.60
Radius of gyration Rg (electron density) rg_electron25.38
Forward intensity I(0) i03741290.00
Molecular weight molecular_weight12173.0 kDa
Excluded volume excluded_volume14291 ų
Envelope volume envelope_volume20178 ų
Hydration-shell volume shell_volume8826 ų
Envelope diameter envelope_diameter90.2
Shell Rg shell_rg25.86
Envelope Rg envelope_rg25.74
Shape Rg shape_rg25.41
Total Rg total_rg25.37
Total atoms total_atoms1543
Residues n_residues113
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 dmax86.7
Rg (real space) rg_real25.41
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real3.7410e+06
I(0) uncertainty (real space) i0_real_error5.5660e+04
Rg (reciprocal space) rg_reciprocal25.23
I(0) (reciprocal space) i0_reciprocal3741000.0000
Solution quality estimate total_estimate0.6444
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary12.4
Skewness Skewness skewness0.619
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83850.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.157; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.014; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)