8z6f

Structure of polycystin-1/polycystin-2 complex with PI(4)P-bound

Method: ELECTRON MICROSCOPY Dmax: 147.6 Å Quality: GOOD

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

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 A; UniProt 3052–4303 Not recorded Polycystin-2 × 3 (Q13563) A1D75 [(2~{R})-2-hexadecanoyloxy-3-[oxidanyl-[(2~{R},3~{R},5~{S},6~{R})-2,3,5,6-tetrakis(oxidanyl)-4-phosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] hexadecanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 1
Chains and sequence ranges Author chain A; PDBConstruct 10–1261; UniProt 3052–4303

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 B; UniProt 1–968 Chain C; UniProt 1–968 Chain D; UniProt 1–968 Not recorded Polycystin-1 × 1 (P98161) A1D75 [(2~{R})-2-hexadecanoyloxy-3-[oxidanyl-[(2~{R},3~{R},5~{S},6~{R})-2,3,5,6-tetrakis(oxidanyl)-4-phosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] hexadecanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 2
Chains and sequence ranges Author chain B; PDBConstruct 40–1007; UniProt 1–968 Author chain C; PDBConstruct 40–1007; UniProt 1–968 Author chain D; PDBConstruct 40–1007; UniProt 1–968

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 8z6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8z6f
Deposition date deposition_date2024-04-19
Structure title titleStructure of polycystin-1/polycystin-2 complex with PI(4)P-bound
Keywords keywordshetero-tetarmer;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_guinier44.03
Radius of gyration Rg (electron density) rg_electron43.13
Forward intensity I(0) i01597500000.00
Molecular weight molecular_weight227270.0 kDa
Excluded volume excluded_volume224270 ų
Envelope volume envelope_volume447050 ų
Hydration-shell volume shell_volume83460 ų
Envelope diameter envelope_diameter158.3
Shell Rg shell_rg50.39
Envelope Rg envelope_rg43.20
Shape Rg shape_rg43.06
Total Rg total_rg43.51
Total atoms total_atoms17376
Residues n_residues2172
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 dmax147.6
Rg (real space) rg_real43.90
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.5970e+09
I(0) uncertainty (real space) i0_real_error2.9870e+07
Rg (reciprocal space) rg_reciprocal44.02
I(0) (reciprocal space) i0_reciprocal1598000000.0000
Solution quality estimate total_estimate0.8577
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis0.012
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha104700000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)