11iy

Protocadherin-15 extracellular domains 1-7

Method: ELECTRON MICROSCOPY Dmax: 239.4 Å Quality: GOOD

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

Protocadherin-15

Mus musculus

UniProt Q99PJ1

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 C; UniProt 28–817 Chain D; UniProt 28–817 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 Å

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.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCD15_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–790; UniProt 28–817 Author chain D; PDBConstruct 1–790; UniProt 28–817

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 11iy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11iy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11iy
Deposition date deposition_date2026-02-26
Structure title titleProtocadherin-15 extracellular domains 1-7
Keywords keywordsTip link, hearing, protocadherin, mechanosensation, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier88.79
Radius of gyration Rg (electron density) rg_electron92.05
Forward intensity I(0) i0444406000.00
Molecular weight molecular_weight175410.0 kDa
Excluded volume excluded_volume218970 ų
Envelope volume envelope_volume368860 ų
Hydration-shell volume shell_volume44702 ų
Envelope diameter envelope_diameter322.4
Shell Rg shell_rg50.72
Envelope Rg envelope_rg92.47
Shape Rg shape_rg92.02
Total Rg total_rg91.27
Total atoms total_atoms24452
Residues n_residues1580
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 dmax239.4
Rg (real space) rg_real80.68
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real4.2230e+08
I(0) uncertainty (real space) i0_real_error9.2540e+06
Rg (reciprocal space) rg_reciprocal79.62
I(0) (reciprocal space) i0_reciprocal432800000.0000
Solution quality estimate total_estimate0.7998
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.9
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.857
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.5398
Highest regularization parameter α highest_alpha14740000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.659; Stabil: 0.965; Sysdev: 1.000; Positv: 1.000; Valcen: 0.565; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)