6n2e

Crystal Structure of Human Protocadherin-15 EC1-3 G16D N369D Q370N and Mouse Cadherin-23 EC1-2 T15E

Method: X-RAY DIFFRACTION Dmax: 170.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Protocadherin-15

Homo sapiens

UniProt A0A087X1T6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 27–396 Chain B; UniProt 27–396 Mutation:G16D, N369D, Q370N Cadherin-23 × 2 (Q99PF4) CA CALCIUM ION × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M Imidazole pH 6.8, 46% MPD Resolution 2.90 Å R-free 0.253

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A087X1T6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–372; UniProt 27–396 Author chain B; PDBConstruct 2–372; UniProt 27–396

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 24–228 Chain D; UniProt 24–228 Mutation:T15E Protocadherin-15 × 2 (A0A087X1T6) CA CALCIUM ION × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M Imidazole pH 6.8, 46% MPD Resolution 2.90 Å R-free 0.253

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 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 6n2e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n2e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n2e
Deposition date deposition_date2018-11-12
Structure title titleCrystal Structure of Human Protocadherin-15 EC1-3 G16D N369D Q370N and Mouse Cadherin-23 EC1-2 T15E
Keywords keywordsMechanotransduction, Calcium-binding protein, stereocilia, hair cell, tip link, 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_guinier46.07
Radius of gyration Rg (electron density) rg_electron47.47
Forward intensity I(0) i0231560000.00
Molecular weight molecular_weight123970.0 kDa
Excluded volume excluded_volume154770 ų
Envelope volume envelope_volume228890 ų
Hydration-shell volume shell_volume45438 ų
Envelope diameter envelope_diameter177.9
Shell Rg shell_rg44.44
Envelope Rg envelope_rg47.11
Shape Rg shape_rg47.52
Total Rg total_rg47.13
Total atoms total_atoms8717
Residues n_residues1099
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 dmax170.3
Rg (real space) rg_real46.83
Rg uncertainty (real space) rg_real_error2.33
I(0) (real space) i0_real2.3160e+08
I(0) uncertainty (real space) i0_real_error3.7950e+06
Rg (reciprocal space) rg_reciprocal46.07
I(0) (reciprocal space) i0_reciprocal231300000.0000
Solution quality estimate total_estimate0.7988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.1
Skewness Skewness skewness0.686
Kurtosis Kurtosis kurtosis0.025
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13010000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.797; Smooth: 0.704

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id6n2eA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3430
Domain ID domain_id6n2eA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3430
Domain ID domain_id6n2eB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id6n2eD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)