6c13

CryoEM structure of mouse PCDH15-4EC-LHFPL5 complex

Method: ELECTRON MICROSCOPY Dmax: 189.9 Å Quality: REASONABLE

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 Other combination Homooligomer Protein × 2 其他Polymer 6 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 821–1465 Chain B; UniProt 821–1465 Not recorded ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.33 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 Q99PJ1-18
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–649; UniProt 821–1465 Author chain B; PDBConstruct 5–649; UniProt 821–1465

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 6c13

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c13
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c13
Deposition date deposition_date2018-01-03
Structure title titleCryoEM structure of mouse PCDH15-4EC-LHFPL5 complex
Keywords keywordsPCDH15, LHFPL5, protocadherin, tip link, hair cell, TMHS, hearing, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.93
Radius of gyration Rg (electron density) rg_electron60.83
Forward intensity I(0) i0223725000.00
Molecular weight molecular_weight125760.0 kDa
Excluded volume excluded_volume158460 ų
Envelope volume envelope_volume265060 ų
Hydration-shell volume shell_volume43753 ų
Envelope diameter envelope_diameter202.8
Shell Rg shell_rg46.99
Envelope Rg envelope_rg59.39
Shape Rg shape_rg60.85
Total Rg total_rg60.18
Total atoms total_atoms8862
Residues n_residues1084
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 dmax189.9
Rg (real space) rg_real60.11
Rg uncertainty (real space) rg_real_error2.32
I(0) (real space) i0_real2.2370e+08
I(0) uncertainty (real space) i0_real_error4.9840e+06
Rg (reciprocal space) rg_reciprocal57.88
I(0) (reciprocal space) i0_reciprocal222900000.0000
Solution quality estimate total_estimate0.7112
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.2
Skewness Skewness skewness0.593
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11530000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.363; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)