4apx

CRYSTAL STRUCTURE OF MOUSE CADHERIN-23 EC1-2 AND PROTOCADHERIN-15 EC1- 2 FORM I

Method: X-RAY DIFFRACTION Dmax: 123.3 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 24–228 Fragment:EC1-2, RESIDUES 24-228 PROTOCADHERIN-15 × 1 (Q99PJ1) CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 K POTASSIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1M MES, 8% PEG8000, PH6.5 Resolution 1.65 Å R-free 0.193

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 2–206; UniProt 24–228

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 27–259 Fragment:EC1-2, RESIDUES 27-259 CADHERIN-23 × 1 (Q99PF4) CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 K POTASSIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1M MES, 8% PEG8000, PH6.5 Resolution 1.65 Å R-free 0.193

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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–234; UniProt 27–259

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 4apx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4apx
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4apx
Deposition date deposition_date2012-04-07
Structure title titleCRYSTAL STRUCTURE OF MOUSE CADHERIN-23 EC1-2 AND PROTOCADHERIN-15 EC1- 2 FORM I
Keywords keywordsCELL ADHESION, HEARING, DEAFNESS, CDH23, PCDH15; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.41
Radius of gyration Rg (electron density) rg_electron33.31
Forward intensity I(0) i041997600.00
Molecular weight molecular_weight50514.0 kDa
Excluded volume excluded_volume62934 ų
Envelope volume envelope_volume83367 ų
Hydration-shell volume shell_volume24312 ų
Envelope diameter envelope_diameter130.2
Shell Rg shell_rg33.94
Envelope Rg envelope_rg33.74
Shape Rg shape_rg33.38
Total Rg total_rg33.13
Total atoms total_atoms3546
Residues n_residues446
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 dmax123.3
Rg (real space) rg_real33.17
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real4.2000e+07
I(0) uncertainty (real space) i0_real_error6.0690e+05
Rg (reciprocal space) rg_reciprocal32.84
I(0) (reciprocal space) i0_reciprocal41990000.0000
Solution quality estimate total_estimate0.7394
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.752
Kurtosis Kurtosis kurtosis0.130
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3573000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.487; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.295; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4apxA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4apxA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4apxB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3430
Domain ID domain_id4apxB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)