7zji

Transient receptor potential cation channel subfamily V member 2,Enhanced green fluorescent protein

Method: ELECTRON MICROSCOPY Dmax: 152.1 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily V member 2,Enhanced green fluorescent protein

Muromegalovirus G4

UniProt A0A0G2JSH6

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 1–761 Chain B; UniProt 1–761 Chain C; UniProt 1–761 Chain D; UniProt 1–761 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G2JSH6_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–761; UniProt 1–761 Author chain B; PDBConstruct 1–761; UniProt 1–761 Author chain C; PDBConstruct 1–761; UniProt 1–761 Author chain D; PDBConstruct 1–761; UniProt 1–761

Transient receptor potential cation channel subfamily V member 2,Enhanced green fluorescent protein

Muromegalovirus G4

UniProt A0A7G8ZY66

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 2–244 Chain B; UniProt 2–244 Chain C; UniProt 2–244 Chain D; UniProt 2–244 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7G8ZY66_MUHV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 776–1018; UniProt 2–244 Author chain B; PDBConstruct 776–1018; UniProt 2–244 Author chain C; PDBConstruct 776–1018; UniProt 2–244 Author chain D; PDBConstruct 776–1018; UniProt 2–244

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 7zji

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7zji
Deposition date deposition_date2022-04-11
Structure title titleTransient receptor potential cation channel subfamily V member 2,Enhanced green fluorescent protein
Keywords keywordsTemperature sensor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.03
Radius of gyration Rg (electron density) rg_electron48.18
Forward intensity I(0) i0924604000.00
Molecular weight molecular_weight272370.0 kDa
Excluded volume excluded_volume348870 ų
Envelope volume envelope_volume521860 ų
Hydration-shell volume shell_volume88164 ų
Envelope diameter envelope_diameter166.9
Shell Rg shell_rg54.89
Envelope Rg envelope_rg47.04
Shape Rg shape_rg48.18
Total Rg total_rg48.47
Total atoms total_atoms19231
Residues n_residues2375
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 dmax152.1
Rg (real space) rg_real48.67
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real9.2460e+08
I(0) uncertainty (real space) i0_real_error1.6520e+07
Rg (reciprocal space) rg_reciprocal49.03
I(0) (reciprocal space) i0_reciprocal925000000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.8
Skewness Skewness skewness0.070
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52570000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.790

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)