3j5p

Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy

Method: ELECTRON MICROSCOPY Dmax: 151.3 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 111–603 Chain A; UniProt 626–718 Chain B; UniProt 111–603 Chain B; UniProt 626–718 Chain C; UniProt 111–603 Chain C; UniProt 626–718 Chain D; UniProt 111–603 Chain D; UniProt 626–718 Fragment:SEE REMARK 999 No other associated polymer 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 3.27 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 626–718 Author chain B; PDBConstruct 1–493; UniProt 111–603 Author chain B; PDBConstruct 494–586; UniProt 626–718 Author chain C; PDBConstruct 1–493; UniProt 111–603 Author chain C; PDBConstruct 494–586; UniProt 626–718 Author chain D; PDBConstruct 1–493; UniProt 111–603 Author chain D; PDBConstruct 494–586; UniProt 626–718

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 3j5p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j5p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j5p
Deposition date deposition_date2013-10-28
Structure title titleStructure of TRPV1 ion channel determined by single particle electron cryo-microscopy
Keywords keywordsTRPV1 channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.42
Radius of gyration Rg (electron density) rg_electron47.47
Forward intensity I(0) i0911830000.00
Molecular weight molecular_weight264230.0 kDa
Excluded volume excluded_volume336040 ų
Envelope volume envelope_volume483970 ų
Hydration-shell volume shell_volume83802 ų
Envelope diameter envelope_diameter156.9
Shell Rg shell_rg53.85
Envelope Rg envelope_rg45.93
Shape Rg shape_rg47.49
Total Rg total_rg47.65
Total atoms total_atoms18636
Residues n_residues2368
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 dmax151.3
Rg (real space) rg_real48.05
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real9.1180e+08
I(0) uncertainty (real space) i0_real_error1.6530e+07
Rg (reciprocal space) rg_reciprocal48.41
I(0) (reciprocal space) i0_reciprocal912200000.0000
Solution quality estimate total_estimate0.8207
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.034
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41110000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3j5pA01
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_id3j5pB01
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_id3j5pC01
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_id3j5pD01
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)