8t1c

Cryo-EM structure of human TRPV4 ankyrin repeat domain in complex with GTPase RhoA

Method: ELECTRON MICROSCOPY Dmax: 87.6 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily V member 4-Enhanced green fluorescent protein chimera

Human cytomegalovirus

UniProt C5MKY7

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–239 Not recorded Transforming protein RhoA × 1 (P61586) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C5MKY7_HCMV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 882–1119; UniProt 2–239

Transient receptor potential cation channel subfamily V member 4-Enhanced green fluorescent protein chimera

Human cytomegalovirus

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–871 Not recorded Transforming protein RhoA × 1 (P61586) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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 1–871; UniProt 1–871

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–193 Not recorded Transient receptor potential cation channel subfamily V member 4-Enhanced green fluorescent protein chimera × 1 (Q9HBA0,C5MKY7) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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

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 8t1c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t1c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t1c
Deposition date deposition_date2023-06-02
Structure title titleCryo-EM structure of human TRPV4 ankyrin repeat domain in complex with GTPase RhoA
Keywords keywords;transient receptor potential V family member 4, TRP, channel, TRPV4, TRP channels, membrane protein, GTPase, transforming protein RhoA, RhoA, ankyrin repeat domain, GDP, guanosine diphosphate ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier23.93
Radius of gyration Rg (electron density) rg_electron22.98
Forward intensity I(0) i032809400.00
Molecular weight molecular_weight43143.0 kDa
Excluded volume excluded_volume53762 ų
Envelope volume envelope_volume66808 ų
Hydration-shell volume shell_volume24726 ų
Envelope diameter envelope_diameter89.6
Shell Rg shell_rg29.50
Envelope Rg envelope_rg23.29
Shape Rg shape_rg22.96
Total Rg total_rg23.85
Total atoms total_atoms6043
Residues n_residues377
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 dmax87.6
Rg (real space) rg_real23.95
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.2810e+07
I(0) uncertainty (real space) i0_real_error4.6530e+05
Rg (reciprocal space) rg_reciprocal23.95
I(0) (reciprocal space) i0_reciprocal32810000.0000
Solution quality estimate total_estimate0.8346
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.0
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.153
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9701000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.870; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8t1cE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)