5un2

Crystal Structure of Mouse Cadherin-23 EC19-21 with non-syndromic deafness (DFNB12) associated mutation R2029W

Method: X-RAY DIFFRACTION Dmax: 157.3 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 A; UniProt 1955–2289 Fragment:residues 1955-2289 Mutation:R2029W CA CALCIUM ION × 8 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;277 K;0.1 M HEPES pH 7.3 0.1 M CaCl2 27% PEG 400 5% glycerol Resolution 2.96 Å R-free 0.236

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 A; PDBConstruct 2–336; UniProt 1955–2289

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 5un2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5un2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5un2
Deposition date deposition_date2017-01-30
Structure title titleCrystal Structure of Mouse Cadherin-23 EC19-21 with non-syndromic deafness (DFNB12) associated mutation R2029W
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_guinier41.78
Radius of gyration Rg (electron density) rg_electron43.68
Forward intensity I(0) i020676000.00
Molecular weight molecular_weight36717.0 kDa
Excluded volume excluded_volume46160 ų
Envelope volume envelope_volume63736 ų
Hydration-shell volume shell_volume16644 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg33.84
Envelope Rg envelope_rg44.39
Shape Rg shape_rg43.62
Total Rg total_rg43.15
Total atoms total_atoms2573
Residues n_residues335
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 dmax157.3
Rg (real space) rg_real42.85
Rg uncertainty (real space) rg_real_error2.95
I(0) (real space) i0_real2.0680e+07
I(0) uncertainty (real space) i0_real_error4.4370e+05
Rg (reciprocal space) rg_reciprocal41.79
I(0) (reciprocal space) i0_reciprocal20650000.0000
Solution quality estimate total_estimate0.5856
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.653
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha601600.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.034; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.013; Smooth: 0.494

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5un2a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.0 — automated matches
Domain ID domain_idd5un2a2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.0 — automated matches
Domain ID domain_idd5un2a3
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5un2A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)