9iqx

Cryo-EM structure of the human TRPV4-RhoA in complex with AH001

Method: ELECTRON MICROSCOPY Dmax: 160.3 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily V member 4

Homo sapiens

UniProt Q9HBA0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 148–787 Chain B; UniProt 148–787 Chain C; UniProt 148–787 Chain D; UniProt 148–787 Not recorded Transforming protein RhoA × 2 (P61586) P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 2 U6L (1~{R})-1-(3-ethylphenyl)ethane-1,2-diol × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPV4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–640; UniProt 148–787 Author chain B; PDBConstruct 1–640; UniProt 148–787 Author chain C; PDBConstruct 1–640; UniProt 148–787 Author chain D; PDBConstruct 1–640; UniProt 148–787

Transforming protein RhoA

Homo sapiens

UniProt P61586

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–193 Chain F; UniProt 1–193 Not recorded Transient receptor potential cation channel subfamily V member 4 × 4 (Q9HBA0) P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 2 U6L (1~{R})-1-(3-ethylphenyl)ethane-1,2-diol × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

129 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–193; UniProt 1–193 Author chain F; PDBConstruct 1–193; UniProt 1–193

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 9iqx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9iqx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9iqx
Deposition date deposition_date2024-07-13
Structure title titleCryo-EM structure of the human TRPV4-RhoA in complex with AH001
Keywords keywordsAntagonist, Complex, MEMBRANE PROTEIN, Hydrolase; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.29
Radius of gyration Rg (electron density) rg_electron50.65
Forward intensity I(0) i02685920000.00
Molecular weight molecular_weight293300.0 kDa
Excluded volume excluded_volume287020 ų
Envelope volume envelope_volume583060 ų
Hydration-shell volume shell_volume94426 ų
Envelope diameter envelope_diameter174.2
Shell Rg shell_rg56.90
Envelope Rg envelope_rg48.54
Shape Rg shape_rg50.61
Total Rg total_rg50.86
Total atoms total_atoms22266
Residues n_residues2770
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 dmax160.3
Rg (real space) rg_real51.03
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real2.6860e+09
I(0) uncertainty (real space) i0_real_error4.9110e+07
Rg (reciprocal space) rg_reciprocal51.50
I(0) (reciprocal space) i0_reciprocal2688000000.0000
Solution quality estimate total_estimate0.8869
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.2
Skewness Skewness skewness0.018
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57230000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.900

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)