4xxw

Crystal structure of mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 splice variant

Method: X-RAY DIFFRACTION Dmax: 170.2 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 27–254 Not recorded Cadherin-23 × 1 (Q99PF4) CA CALCIUM ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Ammonium Acetate 0.1 M HEPES, pH 7.5 25% (v/v) isopropanol Resolution 2.26 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–254 Not recorded Cadherin-23 × 1 (Q99PF4) CA CALCIUM ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Ammonium Acetate 0.1 M HEPES, pH 7.5 25% (v/v) isopropanol Resolution 2.26 Å R-free 0.233

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCD15_MOUSE
Isoform Q99PJ1-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–229; UniProt 27–254 Author chain B; PDBConstruct 2–229; UniProt 27–254

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 24–228 Not recorded Protocadherin-15 × 1 (Q99PJ1) CA CALCIUM ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Ammonium Acetate 0.1 M HEPES, pH 7.5 25% (v/v) isopropanol Resolution 2.26 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 24–228 Not recorded Protocadherin-15 × 1 (Q99PJ1) CA CALCIUM ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Ammonium Acetate 0.1 M HEPES, pH 7.5 25% (v/v) isopropanol Resolution 2.26 Å R-free 0.233

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 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAD23_MOUSE
Isoform Q99PF4-2
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–206; UniProt 24–228 Author chain D; PDBConstruct 2–206; UniProt 24–228

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 4xxw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xxw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xxw
Deposition date deposition_date2015-01-31
Structure title titleCrystal structure of mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 splice variant
Keywords keywordsMechanotransduction, calcium binding protein, cell adhesion, hearing; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.74
Radius of gyration Rg (electron density) rg_electron44.39
Forward intensity I(0) i0143716000.00
Molecular weight molecular_weight96843.0 kDa
Excluded volume excluded_volume120760 ų
Envelope volume envelope_volume187000 ų
Hydration-shell volume shell_volume36960 ų
Envelope diameter envelope_diameter172.2
Shell Rg shell_rg46.75
Envelope Rg envelope_rg42.86
Shape Rg shape_rg44.42
Total Rg total_rg44.42
Total atoms total_atoms6806
Residues n_residues866
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 dmax170.2
Rg (real space) rg_real43.99
Rg uncertainty (real space) rg_real_error2.33
I(0) (real space) i0_real1.4370e+08
I(0) uncertainty (real space) i0_real_error2.9540e+06
Rg (reciprocal space) rg_reciprocal43.74
I(0) (reciprocal space) i0_reciprocal143700000.0000
Solution quality estimate total_estimate0.7035
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.5
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.083
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6438000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.472; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.725; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id4xxwA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3430
Domain ID domain_id4xxwA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4xxwB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3430
Domain ID domain_id4xxwB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4xxwC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4xxwC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4xxwD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4xxwD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)