4cud

Human Notch1 EGF domains 11-13 mutant fucosylated at T466

Method: X-RAY DIFFRACTION Dmax: 100.2 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 410–526 Fragment:EGF 11-13, RESIDUES 410-526 FUC alpha-L-fucopyranose × 2 CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 1.85 Å R-free 0.260

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 2–118; UniProt 410–526

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 4cud

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cud
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cud
Deposition date deposition_date2014-03-18
Structure title titleHuman Notch1 EGF domains 11-13 mutant fucosylated at T466
Keywords keywords;TRANSCRIPTION, METAL-BINDING, TRANSMEMBRANE, DEVELOPMENTAL, PROTEIN, NOTCH SIGNALING PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF-LIKE DOMAIN, REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING, GLYCOPROTEIN, EXTRACELLULAR, EGF, JAGGED, NUCLEUS, MEMBRANE ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.56
Radius of gyration Rg (electron density) rg_electron28.03
Forward intensity I(0) i04173690.00
Molecular weight molecular_weight13567.0 kDa
Excluded volume excluded_volume16215 ų
Envelope volume envelope_volume22589 ų
Hydration-shell volume shell_volume9072 ų
Envelope diameter envelope_diameter103.0
Shell Rg shell_rg26.99
Envelope Rg envelope_rg28.81
Shape Rg shape_rg28.10
Total Rg total_rg27.71
Total atoms total_atoms928
Residues n_residues122
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 dmax100.2
Rg (real space) rg_real27.41
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real4.1740e+06
I(0) uncertainty (real space) i0_real_error7.2170e+04
Rg (reciprocal space) rg_reciprocal27.15
I(0) (reciprocal space) i0_reciprocal4173000.0000
Solution quality estimate total_estimate0.5493
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.4
Skewness Skewness skewness0.662
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86160.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.048; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.006; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4cuda1
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.0 — automated matches
Domain ID domain_idd4cuda2
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.0 — automated matches
Domain ID domain_idd4cuda3
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.0 — automated matches
Domain ID domain_idd4cuda4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id4cudA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id4cudA02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id4cudA03
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)