6a70

Structure of the human PKD1/PKD2 complex

Method: ELECTRON MICROSCOPY Dmax: 146.7 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 185–723 Chain F; UniProt 185–723 Chain G; UniProt 185–723 Not recorded Polycystin-1 × 1 (P98161) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 39–577; UniProt 185–723 Author chain F; PDBConstruct 39–577; UniProt 185–723 Author chain G; PDBConstruct 39–577; UniProt 185–723

Polycystin-1

Homo sapiens

UniProt P98161

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 B; UniProt 3049–4169 Not recorded Polycystin-2 × 3 (Q13563) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PKD1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 33–1153; UniProt 3049–4169

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 6a70

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6a70
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6a70
Deposition date deposition_date2018-06-29
Structure title titleStructure of the human PKD1/PKD2 complex
Keywords keywordsAsymmetric complex, polycystic kidney disease, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.25
Radius of gyration Rg (electron density) rg_electron42.77
Forward intensity I(0) i0649677000.00
Molecular weight molecular_weight213590.0 kDa
Excluded volume excluded_volume268530 ų
Envelope volume envelope_volume422850 ų
Hydration-shell volume shell_volume79870 ų
Envelope diameter envelope_diameter158.2
Shell Rg shell_rg49.67
Envelope Rg envelope_rg42.99
Shape Rg shape_rg42.83
Total Rg total_rg42.92
Total atoms total_atoms15142
Residues n_residues2086
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 dmax146.7
Rg (real space) rg_real44.14
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real6.4970e+08
I(0) uncertainty (real space) i0_real_error1.2180e+07
Rg (reciprocal space) rg_reciprocal44.25
I(0) (reciprocal space) i0_reciprocal649800000.0000
Solution quality estimate total_estimate0.8570
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.1
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis0.014
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81210000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.809

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)