8zl8

Structure of Polycystin-1/Polycystin-2 complex with 7b,27-DHC

Method: ELECTRON MICROSCOPY Dmax: 169.8 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) A1EQ3 (3~{S},7~{R},8~{S},9~{S},10~{R},13~{R},14~{S},17~{R})-10,13-dimethyl-17-[(2~{R},6~{R})-6-methyl-7-oxidanyl-heptan-2-yl]-2,3,4,7,8,9,11,12,14,15,16,17-dodecahydro-1~{H}-cyclopenta[a]phenanthrene-3,7-diol × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.38 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) A1EQ3 (3~{S},7~{R},8~{S},9~{S},10~{R},13~{R},14~{S},17~{R})-10,13-dimethyl-17-[(2~{R},6~{R})-6-methyl-7-oxidanyl-heptan-2-yl]-2,3,4,7,8,9,11,12,14,15,16,17-dodecahydro-1~{H}-cyclopenta[a]phenanthrene-3,7-diol × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.38 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 8zl8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zl8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zl8
Deposition date deposition_date2024-05-17
Structure title titleStructure of Polycystin-1/Polycystin-2 complex with 7b,27-DHC
Keywords keywordsion channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.22
Radius of gyration Rg (electron density) rg_electron45.26
Forward intensity I(0) i01503020000.00
Molecular weight molecular_weight219090.0 kDa
Excluded volume excluded_volume215460 ų
Envelope volume envelope_volume453600 ų
Hydration-shell volume shell_volume82187 ų
Envelope diameter envelope_diameter155.0
Shell Rg shell_rg50.80
Envelope Rg envelope_rg45.17
Shape Rg shape_rg45.21
Total Rg total_rg45.55
Total atoms total_atoms16728
Residues n_residues2176
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 dmax169.8
Rg (real space) rg_real46.06
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real1.5030e+09
I(0) uncertainty (real space) i0_real_error2.9680e+07
Rg (reciprocal space) rg_reciprocal46.22
I(0) (reciprocal space) i0_reciprocal1503000000.0000
Solution quality estimate total_estimate0.7662
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.9
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha98160000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)