8tri

Crystal Structure of Mouse Cadherin-23 EC25-MAD28 F2894A

Method: X-RAY DIFFRACTION Dmax: 251.4 Å Quality: GOOD

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 A; UniProt 2603–3065 Fragment:residues 2603-3065 Mutation:F2894A CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;277 K;1.25 M Lithium Acetate, 0.1 M MES pH 7.2, 25% glycerol (cryo) Resolution 3.72 Å R-free 0.229
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2603–3065 Fragment:residues 2603-3065 Mutation:F2894A CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;277 K;1.25 M Lithium Acetate, 0.1 M MES pH 7.2, 25% glycerol (cryo) Resolution 3.72 Å R-free 0.229
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2603–3065 Fragment:residues 2603-3065 Mutation:F2894A CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;277 K;1.25 M Lithium Acetate, 0.1 M MES pH 7.2, 25% glycerol (cryo) Resolution 3.72 Å R-free 0.229

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 43 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 A; PDBConstruct 4–466; UniProt 2603–3065 Author chain B; PDBConstruct 4–466; UniProt 2603–3065 Author chain C; PDBConstruct 4–466; UniProt 2603–3065

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 8tri

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tri
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tri
Deposition date deposition_date2023-08-09
最后修订 last_revision2024-08-28
Structure title titleCrystal Structure of Mouse Cadherin-23 EC25-MAD28 F2894A
Keywords keywordsHEARING, MECHANOTRANSDUCTION, ADHESION, 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_guinier68.24
Radius of gyration Rg (electron density) rg_electron69.59
Forward intensity I(0) i0322895000.00
Molecular weight molecular_weight149180.0 kDa
Excluded volume excluded_volume186810 ų
Envelope volume envelope_volume337010 ų
Hydration-shell volume shell_volume50369 ų
Envelope diameter envelope_diameter273.4
Shell Rg shell_rg49.94
Envelope Rg envelope_rg68.42
Shape Rg shape_rg69.56
Total Rg total_rg69.01
Total atoms total_atoms10508
Residues n_residues1326
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 dmax251.4
Rg (real space) rg_real68.73
Rg uncertainty (real space) rg_real_error2.73
I(0) (real space) i0_real3.2260e+08
I(0) uncertainty (real space) i0_real_error6.3700e+06
Rg (reciprocal space) rg_reciprocal65.89
I(0) (reciprocal space) i0_reciprocal321200000.0000
Solution quality estimate total_estimate0.7824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.6
Skewness Skewness skewness0.684
Kurtosis Kurtosis kurtosis0.403
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0101
Highest regularization parameter α highest_alpha12450000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.510; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.742; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)