3mvs

Structure of the N-terminus of Cadherin 23

Method: X-RAY DIFFRACTION Dmax: 108.8 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 24–233 Fragment:UNP residues 24-233 CA CALCIUM ION × 6 EDO 1,2-ETHANEDIOL × 22 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;200 nl of 6.9 mg/ml protein in 1 mM CaCl2, 50 mM Tris-HCl, pH 8.5, 200 nl crystallant (22.5% ethylene glycol and 0.2 M NDSB-201), VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.10 Å R-free 0.188

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 1–210; UniProt 24–233

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 3mvs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mvs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mvs
Deposition date deposition_date2010-05-04
Structure title titleStructure of the N-terminus of Cadherin 23
Keywords keywordscadherin, adhesion, extracellular domain, 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_guinier29.22
Radius of gyration Rg (electron density) rg_electron29.70
Forward intensity I(0) i09909350.00
Molecular weight molecular_weight24360.0 kDa
Excluded volume excluded_volume30565 ų
Envelope volume envelope_volume38603 ų
Hydration-shell volume shell_volume13298 ų
Envelope diameter envelope_diameter113.8
Shell Rg shell_rg30.14
Envelope Rg envelope_rg30.07
Shape Rg shape_rg29.57
Total Rg total_rg30.16
Total atoms total_atoms1704
Residues n_residues210
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 dmax108.8
Rg (real space) rg_real29.93
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real9.9090e+06
I(0) uncertainty (real space) i0_real_error1.6490e+05
Rg (reciprocal space) rg_reciprocal29.63
I(0) (reciprocal space) i0_reciprocal9907000.0000
Solution quality estimate total_estimate0.6512
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.683
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha591200.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.173; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.026; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3mvsA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id3mvsA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)