9p3d

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

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin, alpha skeletal muscle

Oryctolagus cuniculus

UniProt P68135

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 22 Vibrio VopV × 11 (A0A250E4R0) MAGNESIUM ION × 11 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 11 water × 11 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 22 Actin, alpha skeletal muscle × 11 (P68135) MAGNESIUM ION × 11 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 11 water × 11 Consistent with protein count

Other States of the Same Protein in the Database

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.

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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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9p3d__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9p3d__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9p3d__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)88.10 Å
Rg (electron density)90.96 Å
Total Rg90.47 Å
Atom count36388
Residues4609
Excluded volume645840 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9p3d__assembly_1__model_1 22-meric (22) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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7. Citations (1)