5fm9

human Notch 1, EGF 4-7

Method: X-RAY DIFFRACTION Dmax: 90.8 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 140–294 Fragment:EGF DOMAINS 4-7, UNP RESIDUES 140-294 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;PH 8.5 Resolution 2.92 Å R-free 0.237

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 3–157; UniProt 140–294

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 5fm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fm9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fm9
Deposition date deposition_date2015-11-02
Structure title titlehuman Notch 1, EGF 4-7
Keywords keywords;TRANSCRIPTION, TRANSMEMBRANE, DEVELOPMENTAL, PROTEIN, NOTCH SIGNALING PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF- LIKE DOMAIN, REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING, GLYCOPROTEIN, EXTRACELLULAR, EGF, NOTCH, JAGGED, MEMBRANE ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.00
Radius of gyration Rg (electron density) rg_electron28.34
Forward intensity I(0) i06217520.00
Molecular weight molecular_weight16398.0 kDa
Excluded volume excluded_volume19283 ų
Envelope volume envelope_volume31153 ų
Hydration-shell volume shell_volume10245 ų
Envelope diameter envelope_diameter91.2
Shell Rg shell_rg32.45
Envelope Rg envelope_rg26.98
Shape Rg shape_rg28.40
Total Rg total_rg28.63
Total atoms total_atoms1127
Residues n_residues154
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 dmax90.8
Rg (real space) rg_real28.33
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real6.2180e+06
I(0) uncertainty (real space) i0_real_error1.0470e+05
Rg (reciprocal space) rg_reciprocal28.24
I(0) (reciprocal space) i0_reciprocal6217000.0000
Solution quality estimate total_estimate0.7161
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary12.7
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-1.032
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97850.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.392; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.242; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)