6o1u

Cryo-EM structure of TRPV5 W583A in nanodisc

Method: ELECTRON MICROSCOPY Dmax: 140.2 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily V member 5

Oryctolagus cuniculus

UniProt Q9XSM3

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 1–730 Chain B; UniProt 1–730 Chain C; UniProt 1–730 Chain D; UniProt 1–730 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPV5_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–730; UniProt 1–730 Author chain B; PDBConstruct 1–730; UniProt 1–730 Author chain C; PDBConstruct 1–730; UniProt 1–730 Author chain D; PDBConstruct 1–730; UniProt 1–730

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 6o1u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o1u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6o1u
Deposition date deposition_date2019-02-21
Structure title titleCryo-EM structure of TRPV5 W583A in nanodisc
Keywords keywordsion channel, TRP channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.10
Radius of gyration Rg (electron density) rg_electron46.02
Forward intensity I(0) i01047970000.00
Molecular weight molecular_weight278830.0 kDa
Excluded volume excluded_volume352920 ų
Envelope volume envelope_volume489350 ų
Hydration-shell volume shell_volume85454 ų
Envelope diameter envelope_diameter143.3
Shell Rg shell_rg54.00
Envelope Rg envelope_rg44.67
Shape Rg shape_rg46.03
Total Rg total_rg46.33
Total atoms total_atoms19612
Residues n_residues2456
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 dmax140.2
Rg (real space) rg_real46.68
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.0480e+09
I(0) uncertainty (real space) i0_real_error1.7750e+07
Rg (reciprocal space) rg_reciprocal47.10
I(0) (reciprocal space) i0_reciprocal1048000000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.7
Skewness Skewness skewness-0.057
Kurtosis Kurtosis kurtosis-0.593
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48480000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.775

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_id6o1uA01
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_id6o1uB01
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_id6o1uC01
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_id6o1uD01
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)