7x6i

Cryo-EM structure of the human TRPC5 ion channel in complex with G alpha i3 subunits, class1

Method: ELECTRON MICROSCOPY Dmax: 197.5 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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) 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 Guanine nucleotide-binding protein G(i) subunit alpha-3 × 4 (P08754) PTY PHOSPHATIDYLETHANOLAMINE × 4 Y01 CHOLESTEROL HEMISUCCINATE × 4 ZN ZINC ION × 4 CA CALCIUM ION × 4 YZY (2S)-2-(hexadecanoyloxy)-3-hydroxypropyl (9Z)-octadec-9-enoate × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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

Guanine nucleotide-binding protein G(i) subunit alpha-3

Homo sapiens

UniProt P08754

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–119 Chain E; UniProt 120–354 Chain F; UniProt 1–119 Chain F; UniProt 120–354 Chain G; UniProt 1–119 Chain G; UniProt 120–354 Chain H; UniProt 1–119 Chain H; UniProt 120–354 Mutation:Q204L Short transient receptor potential channel 5 × 4 (Q9UL62) PTY PHOSPHATIDYLETHANOLAMINE × 4 Y01 CHOLESTEROL HEMISUCCINATE × 4 ZN ZINC ION × 4 CA CALCIUM ION × 4 YZY (2S)-2-(hexadecanoyloxy)-3-hydroxypropyl (9Z)-octadec-9-enoate × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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.

24 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–119; UniProt 1–119 Author chain E; PDBConstruct 126–360; UniProt 120–354 Author chain F; PDBConstruct 1–119; UniProt 1–119 Author chain F; PDBConstruct 126–360; UniProt 120–354 Author chain G; PDBConstruct 1–119; UniProt 1–119 Author chain G; PDBConstruct 126–360; UniProt 120–354 Author chain H; PDBConstruct 1–119; UniProt 1–119 Author chain H; PDBConstruct 126–360; UniProt 120–354

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 7x6i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7x6i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7x6i
Deposition date deposition_date2022-03-07
Structure title titleCryo-EM structure of the human TRPC5 ion channel in complex with G alpha i3 subunits, class1
Keywords keywordstransient receptor potential, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.46
Radius of gyration Rg (electron density) rg_electron58.90
Forward intensity I(0) i02830940000.00
Molecular weight molecular_weight467100.0 kDa
Excluded volume excluded_volume592890 ų
Envelope volume envelope_volume884830 ų
Hydration-shell volume shell_volume127010 ų
Envelope diameter envelope_diameter190.4
Shell Rg shell_rg59.47
Envelope Rg envelope_rg57.43
Shape Rg shape_rg58.93
Total Rg total_rg58.82
Total atoms total_atoms32908
Residues n_residues3968
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 dmax197.5
Rg (real space) rg_real59.28
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real2.8310e+09
I(0) uncertainty (real space) i0_real_error6.2100e+07
Rg (reciprocal space) rg_reciprocal59.60
I(0) (reciprocal space) i0_reciprocal2832000000.0000
Solution quality estimate total_estimate0.8688
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.0
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha132700000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.752

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)