7s8c

Cryo-EM structure of human TRPV6 in complex with inhibitor econazole

Method: ELECTRON MICROSCOPY Dmax: 140.7 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily V member 6

Homo sapiens

UniProt Q9H1D0

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 41–707 Chain B; UniProt 41–707 Chain C; UniProt 41–707 Chain D; UniProt 41–707 Not recorded ECL 1-[(2R)-2-[(4-chlorobenzyl)oxy]-2-(2,4-dichlorophenyl)ethyl]-1H-imidazole × 4 Y01 CHOLESTEROL HEMISUCCINATE × 12 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 16 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.85 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPV6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–667; UniProt 41–707 Author chain B; PDBConstruct 1–667; UniProt 41–707 Author chain C; PDBConstruct 1–667; UniProt 41–707 Author chain D; PDBConstruct 1–667; UniProt 41–707

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 7s8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s8c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s8c
Deposition date deposition_date2021-09-17
Structure title titleCryo-EM structure of human TRPV6 in complex with inhibitor econazole
Keywords keywords;Transient Receptor Potential V Family Member 6, TRP, channel, econazole, inhibitor, antagonist, cNW11, nanodiscs, TRPV6, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.29
Radius of gyration Rg (electron density) rg_electron46.04
Forward intensity I(0) i01067020000.00
Molecular weight molecular_weight292820.0 kDa
Excluded volume excluded_volume375190 ų
Envelope volume envelope_volume502810 ų
Hydration-shell volume shell_volume87587 ų
Envelope diameter envelope_diameter145.5
Shell Rg shell_rg53.83
Envelope Rg envelope_rg44.96
Shape Rg shape_rg46.04
Total Rg total_rg46.33
Total atoms total_atoms20562
Residues n_residues2448
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 dmax140.7
Rg (real space) rg_real46.88
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real1.0670e+09
I(0) uncertainty (real space) i0_real_error1.8390e+07
Rg (reciprocal space) rg_reciprocal47.28
I(0) (reciprocal space) i0_reciprocal1068000000.0000
Solution quality estimate total_estimate0.8864
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.0
Skewness Skewness skewness-0.034
Kurtosis Kurtosis kurtosis-0.579
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha54060000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.739

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7s8cA01
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_id7s8cB01
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_id7s8cC01
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_id7s8cD01
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)