9dwt

PKD2 ion channel, F634A mutant

Method: ELECTRON MICROSCOPY Dmax: 113.8 Å Quality: EXCELLENT

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

Polycystin-2

Homo sapiens

UniProt Q13563

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 214–693 Chain B; UniProt 214–693 Chain C; UniProt 214–693 Chain D; UniProt 214–693 Mutation:F634A CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;25 mM HEPES-NaOH, 150 mM NaCl, 1 mM CaCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE;Vitrification carried in air. Ethane temperature -183 C Resolution 3.01 Å

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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PKD2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–480; UniProt 214–693 Author chain B; PDBConstruct 1–480; UniProt 214–693 Author chain C; PDBConstruct 1–480; UniProt 214–693 Author chain D; PDBConstruct 1–480; UniProt 214–693

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 9dwt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dwt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9dwt
Deposition date deposition_date2024-10-10
Structure title titlePKD2 ion channel, F634A mutant
Keywords keywordsIon channel, TRP channel, polycystin, membrane protein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.85
Radius of gyration Rg (electron density) rg_electron37.62
Forward intensity I(0) i0585677000.00
Molecular weight molecular_weight214760.0 kDa
Excluded volume excluded_volume275000 ų
Envelope volume envelope_volume359290 ų
Hydration-shell volume shell_volume74729 ų
Envelope diameter envelope_diameter118.5
Shell Rg shell_rg47.45
Envelope Rg envelope_rg37.26
Shape Rg shape_rg37.60
Total Rg total_rg38.31
Total atoms total_atoms30229
Residues n_residues1844
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 dmax113.8
Rg (real space) rg_real38.46
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real5.8570e+08
I(0) uncertainty (real space) i0_real_error8.9160e+06
Rg (reciprocal space) rg_reciprocal38.70
I(0) (reciprocal space) i0_reciprocal585800000.0000
Solution quality estimate total_estimate0.9010
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.7
Skewness Skewness skewness-0.034
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117500000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)