3j5q

Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy

Method: ELECTRON MICROSCOPY Dmax: 149.4 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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 111–719 Chain D; UniProt 111–719 Chain E; UniProt 111–719 Chain G; UniProt 111–719 Fragment:SEE REMARK 999 Kappa-theraphotoxin-Cg1a 1 × 4 (P0C247) ELECTRON MICROSCOPY cryo-EM buffer:150 mM NaCl, 20 mM HEPES, 2 mM TCEP;pH 7.4;150 mM NaCl, 20 mM HEPES, 2 mM TCEP cryo-EM vitrification conditions:Blot for 6 sec;120 K;Cryogen ETHANE;Blot for 6 seconds before plunging into liquid ethane (FEI VITROBOT MARK III) Resolution 3.80 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 B; PDBConstruct 1–586; UniProt 111–719 Author chain D; PDBConstruct 1–586; UniProt 111–719 Author chain E; PDBConstruct 1–586; UniProt 111–719 Author chain G; PDBConstruct 1–586; UniProt 111–719

Kappa-theraphotoxin-Cg1a 1

OrganismNot specified

UniProt P0C247

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 51–81 Chain C; UniProt 51–81 Chain F; UniProt 51–81 Chain H; UniProt 51–81 Fragment:UNP residues 51-81 Transient receptor potential cation channel subfamily V member 1 × 4 (O35433) ELECTRON MICROSCOPY cryo-EM buffer:150 mM NaCl, 20 mM HEPES, 2 mM TCEP;pH 7.4;150 mM NaCl, 20 mM HEPES, 2 mM TCEP cryo-EM vitrification conditions:Blot for 6 sec;120 K;Cryogen ETHANE;Blot for 6 seconds before plunging into liquid ethane (FEI VITROBOT MARK III) Resolution 3.80 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name JZ11A_CHIGU
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–31; UniProt 51–81 Author chain C; PDBConstruct 1–31; UniProt 51–81 Author chain F; PDBConstruct 1–31; UniProt 51–81 Author chain H; PDBConstruct 1–31; UniProt 51–81

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 3j5q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j5q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j5q
Deposition date deposition_date2013-10-28
Structure title titleStructure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy
Keywords keywordsTRPV1 channel, DkTx, RTX, TRANSPORT PROTEIN-TOXIN complex; TRANSPORT PROTEIN/TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.17
Radius of gyration Rg (electron density) rg_electron47.06
Forward intensity I(0) i0932450000.00
Molecular weight molecular_weight258800.0 kDa
Excluded volume excluded_volume325510 ų
Envelope volume envelope_volume485390 ų
Hydration-shell volume shell_volume84655 ų
Envelope diameter envelope_diameter153.1
Shell Rg shell_rg53.48
Envelope Rg envelope_rg45.43
Shape Rg shape_rg47.06
Total Rg total_rg47.35
Total atoms total_atoms18556
Residues n_residues2492
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 dmax149.4
Rg (real space) rg_real47.78
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real9.3240e+08
I(0) uncertainty (real space) i0_real_error1.6570e+07
Rg (reciprocal space) rg_reciprocal48.17
I(0) (reciprocal space) i0_reciprocal932900000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.4
Skewness Skewness skewness0.012
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51300000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3j5qB01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id3j5qD01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id3j5qE01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id3j5qG01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (1)

9. Files and Curves (10)