7mzb

Cryo-EM structure of minimal TRPV1 with 3 bound RTX and 1 perturbed PI

Method: ELECTRON MICROSCOPY Dmax: 132.6 Å Quality: GOOD

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 110–764 Chain B; UniProt 110–764 Chain C; UniProt 110–764 Chain D; UniProt 110–764 Fragment:UNP residues 110-764 XJ7 (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propan-2-yl tridecanoate × 1 6EU resiniferatoxin × 3 NA SODIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.85 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.72 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 6–637; UniProt 110–764 Author chain B; PDBConstruct 6–637; UniProt 110–764 Author chain C; PDBConstruct 6–637; UniProt 110–764 Author chain D; PDBConstruct 6–637; UniProt 110–764

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 7mzb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7mzb
Deposition date deposition_date2021-05-24
Structure title titleCryo-EM structure of minimal TRPV1 with 3 bound RTX and 1 perturbed PI
Keywords keywordsTRP channel, cryo-EM, nanodisc, stoichiometry, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.20
Radius of gyration Rg (electron density) rg_electron43.29
Forward intensity I(0) i0784247000.00
Molecular weight molecular_weight249500.0 kDa
Excluded volume excluded_volume319310 ų
Envelope volume envelope_volume441180 ų
Hydration-shell volume shell_volume81530 ų
Envelope diameter envelope_diameter137.4
Shell Rg shell_rg51.72
Envelope Rg envelope_rg42.09
Shape Rg shape_rg43.32
Total Rg total_rg43.58
Total atoms total_atoms17607
Residues n_residues2145
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 dmax132.6
Rg (real space) rg_real43.84
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real7.8420e+08
I(0) uncertainty (real space) i0_real_error1.3850e+07
Rg (reciprocal space) rg_reciprocal44.20
I(0) (reciprocal space) i0_reciprocal784600000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.6
Skewness Skewness skewness-0.047
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50000000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)