3j9j

Structure of the capsaicin receptor, TRPV1, determined by single particle electron cryo-microscopy

Method: ELECTRON MICROSCOPY Dmax: 108.0 Å Quality: REASONABLE

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

Transient receptor potential cation channel subfamily V member 1

Rattus norvegicus

UniProt O35433

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 111–603 Chain A; UniProt 627–719 Chain B; UniProt 111–603 Chain B; UniProt 627–719 Chain C; UniProt 111–603 Chain C; UniProt 627–719 Chain D; UniProt 111–603 Chain D; UniProt 627–719 Fragment:SEE REMARK 999 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPV1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–493; UniProt 111–603 Author chain A; PDBConstruct 494–586; UniProt 627–719 Author chain B; PDBConstruct 1–493; UniProt 111–603 Author chain B; PDBConstruct 494–586; UniProt 627–719 Author chain C; PDBConstruct 1–493; UniProt 111–603 Author chain C; PDBConstruct 494–586; UniProt 627–719 Author chain D; PDBConstruct 1–493; UniProt 111–603 Author chain D; PDBConstruct 494–586; UniProt 627–719

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 3j9j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j9j
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3j9j
Deposition date deposition_date2015-02-02
Structure title titleStructure of the capsaicin receptor, TRPV1, determined by single particle electron cryo-microscopy
Keywords keywordsalpha helical, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.29
Radius of gyration Rg (electron density) rg_electron35.23
Forward intensity I(0) i0272214000.00
Molecular weight molecular_weight148160.0 kDa
Excluded volume excluded_volume191290 ų
Envelope volume envelope_volume241980 ų
Hydration-shell volume shell_volume55340 ų
Envelope diameter envelope_diameter115.8
Shell Rg shell_rg43.15
Envelope Rg envelope_rg35.47
Shape Rg shape_rg35.23
Total Rg total_rg35.84
Total atoms total_atoms21068
Residues n_residues1260
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 dmax108.0
Rg (real space) rg_real36.05
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real2.7220e+08
I(0) uncertainty (real space) i0_real_error4.1730e+06
Rg (reciprocal space) rg_reciprocal36.20
I(0) (reciprocal space) i0_reciprocal272300000.0000
Solution quality estimate total_estimate0.6659
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.1
Skewness Skewness skewness0.082
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45130000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 0.028; Positv: 1.000; Valcen: 0.978; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)