6c10

Crystal structure of mouse PCDH15 EC11-EL

Method: X-RAY DIFFRACTION Dmax: 71.6 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1151–1388 Not recorded MAN alpha-D-mannopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.2 M Lithium sulfate, 30% (w/v) PEG4000, 0.1 M Tris pH 8.5 Resolution 1.40 Å R-free 0.195

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 Q99PJ1-10
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–241; UniProt 1151–1388

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 6c10

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c10
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c10
Deposition date deposition_date2018-01-03
Structure title titleCrystal structure of mouse PCDH15 EC11-EL
Keywords keywordsPCDH15, LHFPL5, protocadherin, tip link, hair cell, TMHS, hearing, membrane protein, metal transport; membrane protein, metal transport
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.80
Radius of gyration Rg (electron density) rg_electron19.65
Forward intensity I(0) i013209600.00
Molecular weight molecular_weight27615.0 kDa
Excluded volume excluded_volume34825 ų
Envelope volume envelope_volume42414 ų
Hydration-shell volume shell_volume18623 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg25.44
Envelope Rg envelope_rg19.91
Shape Rg shape_rg19.64
Total Rg total_rg20.54
Total atoms total_atoms1946
Residues n_residues244
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 dmax71.6
Rg (real space) rg_real20.78
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.3210e+07
I(0) uncertainty (real space) i0_real_error1.8440e+05
Rg (reciprocal space) rg_reciprocal20.79
I(0) (reciprocal space) i0_reciprocal13210000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2483000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)