9w4t

ratTRPV1 bound with antagonist AMG9810

Method: ELECTRON MICROSCOPY Dmax: 132.6 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,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 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–838 Chain B; UniProt 1–838 Chain C; UniProt 1–838 Chain D; UniProt 1–838 Not recorded A1D6W (~{Z})-3-(4-~{tert}-butylphenyl)-~{N}-(2,3-dihydro-1,4-benzodioxin-6-yl)prop-2-enamide × 4 NA SODIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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 415–1252; UniProt 1–838 Author chain B; PDBConstruct 415–1252; UniProt 1–838 Author chain C; PDBConstruct 415–1252; UniProt 1–838 Author chain D; PDBConstruct 415–1252; UniProt 1–838

Maltose/maltodextrin-binding periplasmic protein,Transient receptor potential cation channel subfamily V member 1

Rattus norvegicus

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Chain C; UniProt 27–392 Chain D; UniProt 27–392 Not recorded A1D6W (~{Z})-3-(4-~{tert}-butylphenyl)-~{N}-(2,3-dihydro-1,4-benzodioxin-6-yl)prop-2-enamide × 4 NA SODIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392 Author chain B; PDBConstruct 2–367; UniProt 27–392 Author chain C; PDBConstruct 2–367; UniProt 27–392 Author chain D; PDBConstruct 2–367; UniProt 27–392

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 9w4t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w4t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9w4t
Deposition date deposition_date2025-08-01
Structure title titleratTRPV1 bound with antagonist AMG9810
Keywords keywordsantagonist, complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.20
Radius of gyration Rg (electron density) rg_electron43.33
Forward intensity I(0) i0776842000.00
Molecular weight molecular_weight248240.0 kDa
Excluded volume excluded_volume317560 ų
Envelope volume envelope_volume437800 ų
Hydration-shell volume shell_volume80811 ų
Envelope diameter envelope_diameter135.9
Shell Rg shell_rg51.60
Envelope Rg envelope_rg42.16
Shape Rg shape_rg43.32
Total Rg total_rg43.73
Total atoms total_atoms35089
Residues n_residues2148
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_error0.94
I(0) (real space) i0_real7.7680e+08
I(0) uncertainty (real space) i0_real_error1.4640e+07
Rg (reciprocal space) rg_reciprocal44.19
I(0) (reciprocal space) i0_reciprocal777200000.0000
Solution quality estimate total_estimate0.8901
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.6
Skewness Skewness skewness-0.044
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49190000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.875

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)