9rro

Human TRPC5 in complex with (-) englerin A, full occupancy, intermediary desensitized state

Method: ELECTRON MICROSCOPY Dmax: 140.5 Å Quality: GOOD

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

Short transient receptor potential channel 5

Homo sapiens

UniProt Q9UL62

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 1–765 Chain B; UniProt 1–765 Chain C; UniProt 1–765 Chain D; UniProt 1–765 Not recorded CA CALCIUM ION × 4 ZN ZINC ION × 4 PTY PHOSPHATIDYLETHANOLAMINE × 4 Y01 CHOLESTEROL HEMISUCCINATE × 4 A1L55 (-)-englerin A × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPC5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–765; UniProt 1–765 Author chain B; PDBConstruct 1–765; UniProt 1–765 Author chain C; PDBConstruct 1–765; UniProt 1–765 Author chain D; PDBConstruct 1–765; UniProt 1–765

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 9rro

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rro
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rro
Deposition date deposition_date2025-06-27
Structure title titleHuman TRPC5 in complex with (-) englerin A, full occupancy, intermediary desensitized state
Keywords keywordsTRPC5, (-) englerin A, agonist, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.97
Radius of gyration Rg (electron density) rg_electron44.10
Forward intensity I(0) i02766960000.00
Molecular weight molecular_weight302510.0 kDa
Excluded volume excluded_volume300190 ų
Envelope volume envelope_volume563520 ų
Hydration-shell volume shell_volume100980 ų
Envelope diameter envelope_diameter142.9
Shell Rg shell_rg53.33
Envelope Rg envelope_rg42.97
Shape Rg shape_rg43.88
Total Rg total_rg44.79
Total atoms total_atoms23572
Residues n_residues2752
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 dmax140.5
Rg (real space) rg_real44.65
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.7670e+09
I(0) uncertainty (real space) i0_real_error4.3580e+07
Rg (reciprocal space) rg_reciprocal44.97
I(0) (reciprocal space) i0_reciprocal2768000000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.2
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha175300000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.903

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)