9p3d

cryo-EM structure of Vibrio effector VopV fragment bound to skeletal alpha F-actin

Method: ELECTRON MICROSCOPY Dmax: 244.4 Å Quality: GOOD

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

Actin, alpha skeletal muscle

Oryctolagus cuniculus

UniProt P68135

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain Q; UniProt 6–377 Chain R; UniProt 6–377 Chain S; UniProt 6–377 Chain T; UniProt 6–377 Chain U; UniProt 6–377 Chain V; UniProt 6–377 Chain W; UniProt 6–377 Chain X; UniProt 6–377 Chain Y; UniProt 6–377 Chain Z; UniProt 6–377 Chain a; UniProt 6–377 Not recorded Vibrio VopV × 11 (A0A250E4R0) MG MAGNESIUM ION × 11 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain Q; PDBConstruct 1–372; UniProt 6–377 Author chain R; PDBConstruct 1–372; UniProt 6–377 Author chain S; PDBConstruct 1–372; UniProt 6–377 Author chain T; PDBConstruct 1–372; UniProt 6–377 Author chain U; PDBConstruct 1–372; UniProt 6–377 Author chain V; PDBConstruct 1–372; UniProt 6–377 Author chain W; PDBConstruct 1–372; UniProt 6–377 Author chain X; PDBConstruct 1–372; UniProt 6–377 Author chain Y; PDBConstruct 1–372; UniProt 6–377 Author chain Z; PDBConstruct 1–372; UniProt 6–377 Author chain a; PDBConstruct 1–372; UniProt 6–377

Vibrio VopV

Vibrio cholerae

UniProt A0A250E4R0

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain c; UniProt 352–398 Chain d; UniProt 352–398 Chain e; UniProt 352–398 Chain f; UniProt 352–398 Chain g; UniProt 352–398 Chain h; UniProt 352–398 Chain i; UniProt 352–398 Chain j; UniProt 352–398 Chain k; UniProt 352–398 Chain l; UniProt 352–398 Chain m; UniProt 352–398 Not recorded Actin, alpha skeletal muscle × 11 (P68135) MG MAGNESIUM ION × 11 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A250E4R0_VIBPH
Isoform
PDB entities 2
Chains and sequence ranges Author chain c; PDBConstruct 1–47; UniProt 352–398 Author chain d; PDBConstruct 1–47; UniProt 352–398 Author chain e; PDBConstruct 1–47; UniProt 352–398 Author chain f; PDBConstruct 1–47; UniProt 352–398 Author chain g; PDBConstruct 1–47; UniProt 352–398 Author chain h; PDBConstruct 1–47; UniProt 352–398 Author chain i; PDBConstruct 1–47; UniProt 352–398 Author chain j; PDBConstruct 1–47; UniProt 352–398 Author chain k; PDBConstruct 1–47; UniProt 352–398 Author chain l; PDBConstruct 1–47; UniProt 352–398 Author chain m; PDBConstruct 1–47; UniProt 352–398

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 9p3d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p3d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p3d
Deposition date deposition_date2025-06-13
Structure title titlecryo-EM structure of Vibrio effector VopV fragment bound to skeletal alpha F-actin
Keywords keywordsT3SS, actin binding, Vibrio effector proteins, actin isoforms, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier88.10
Radius of gyration Rg (electron density) rg_electron90.96
Forward intensity I(0) i03937480000.00
Molecular weight molecular_weight519540.0 kDa
Excluded volume excluded_volume645840 ų
Envelope volume envelope_volume919200 ų
Hydration-shell volume shell_volume101610 ų
Envelope diameter envelope_diameter350.5
Shell Rg shell_rg58.33
Envelope Rg envelope_rg92.50
Shape Rg shape_rg90.97
Total Rg total_rg90.47
Total atoms total_atoms36388
Residues n_residues4609
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 dmax244.4
Rg (real space) rg_real81.02
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real3.7600e+09
I(0) uncertainty (real space) i0_real_error7.7530e+07
Rg (reciprocal space) rg_reciprocal79.86
I(0) (reciprocal space) i0_reciprocal3845000000.0000
Solution quality estimate total_estimate0.8191
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.3
Skewness Skewness skewness0.468
Kurtosis Kurtosis kurtosis-0.789
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.5675
Highest regularization parameter α highest_alpha65170000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.657; Stabil: 0.963; Sysdev: 1.000; Positv: 1.000; Valcen: 0.843; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)