7u71

Crystal Structure of Mouse Cadherin-23 EC13-15

Method: X-RAY DIFFRACTION Dmax: 144.2 Å Quality: REASONABLE

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

Cadherin-23

Mus musculus

UniProt Q99PF4

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 AAA; UniProt 1308–1628 Fragment:UNP residuess 1308-1628 CA CALCIUM ION × 6 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.1 M HEPES pH7.5 0.2 M NaOAc 20% PEG 3000 Resolution 1.98 Å R-free 0.221

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 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAD23_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 2–322; UniProt 1308–1628

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 7u71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7u71
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7u71
Deposition date deposition_date2022-03-07
Structure title titleCrystal Structure of Mouse Cadherin-23 EC13-15
Keywords keywordsHEARING, MECHANOTRANSDUCTION, CALCIUM-BINDING PROTEIN, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.31
Radius of gyration Rg (electron density) rg_electron40.26
Forward intensity I(0) i017989200.00
Molecular weight molecular_weight32968.0 kDa
Excluded volume excluded_volume41096 ų
Envelope volume envelope_volume56215 ų
Hydration-shell volume shell_volume16046 ų
Envelope diameter envelope_diameter142.8
Shell Rg shell_rg32.10
Envelope Rg envelope_rg41.03
Shape Rg shape_rg40.34
Total Rg total_rg39.36
Total atoms total_atoms2314
Residues n_residues300
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 dmax144.2
Rg (real space) rg_real39.67
Rg uncertainty (real space) rg_real_error2.60
I(0) (real space) i0_real1.7990e+07
I(0) uncertainty (real space) i0_real_error3.5410e+05
Rg (reciprocal space) rg_reciprocal38.83
I(0) (reciprocal space) i0_reciprocal17970000.0000
Solution quality estimate total_estimate0.5858
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.669
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha503800.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.033; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.009; Smooth: 0.506

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)