9rsg

Human TRPC5 in complex with (-) englerin A, mixed occupancy_2, state 2

Method: ELECTRON MICROSCOPY Dmax: 131.5 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 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 9rsg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rsg
Deposition date deposition_date2025-07-01
Structure title titleHuman TRPC5 in complex with (-) englerin A, mixed occupancy_2, state 2
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_guinier43.48
Radius of gyration Rg (electron density) rg_electron42.54
Forward intensity I(0) i0922424000.00
Molecular weight molecular_weight267590.0 kDa
Excluded volume excluded_volume341720 ų
Envelope volume envelope_volume482750 ų
Hydration-shell volume shell_volume89956 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg51.79
Envelope Rg envelope_rg41.35
Shape Rg shape_rg42.53
Total Rg total_rg43.02
Total atoms total_atoms18856
Residues n_residues2313
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 dmax131.5
Rg (real space) rg_real43.15
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real9.2240e+08
I(0) uncertainty (real space) i0_real_error1.3850e+07
Rg (reciprocal space) rg_reciprocal43.48
I(0) (reciprocal space) i0_reciprocal922800000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.4
Skewness Skewness skewness0.012
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha99380000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)