7z7h

Structure of P. luminescens TccC3-F-actin complex

Method: ELECTRON MICROSCOPY Dmax: 176.7 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–377 Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Chain E; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose/maltodextrin-binding periplasmic protein,TccC3 × 1 (P0AEX9,Q8GF97) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 APR ADENOSINE-5-DIPHOSPHORIBOSE × 1 NCA NICOTINAMIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 A; PDBConstruct 1–377; UniProt 1–377 Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain D; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377

Maltose/maltodextrin-binding periplasmic protein,TccC3

Photorhabdus luminescens

UniProt P0AEX9

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 27–392 Not recorded Actin, alpha skeletal muscle × 5 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 APR ADENOSINE-5-DIPHOSPHORIBOSE × 1 NCA NICOTINAMIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 22–387; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,TccC3

Photorhabdus luminescens

UniProt Q8GF97

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 779–960 Not recorded Actin, alpha skeletal muscle × 5 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 APR ADENOSINE-5-DIPHOSPHORIBOSE × 1 NCA NICOTINAMIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8GF97_PHOLU
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 397–578; UniProt 779–960

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 7z7h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z7h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z7h
Deposition date deposition_date2022-03-15
Structure title titleStructure of P. luminescens TccC3-F-actin complex
Keywords keywordsBacterial toxin, F-actin, toxin; TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.03
Radius of gyration Rg (electron density) rg_electron48.49
Forward intensity I(0) i0788148000.00
Molecular weight molecular_weight229840.0 kDa
Excluded volume excluded_volume286810 ų
Envelope volume envelope_volume402720 ų
Hydration-shell volume shell_volume72515 ų
Envelope diameter envelope_diameter191.8
Shell Rg shell_rg49.05
Envelope Rg envelope_rg48.12
Shape Rg shape_rg48.49
Total Rg total_rg48.48
Total atoms total_atoms16111
Residues n_residues2031
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 dmax176.7
Rg (real space) rg_real48.44
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real7.8810e+08
I(0) uncertainty (real space) i0_real_error1.6320e+07
Rg (reciprocal space) rg_reciprocal48.04
I(0) (reciprocal space) i0_reciprocal787700000.0000
Solution quality estimate total_estimate0.8309
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.566
Kurtosis Kurtosis kurtosis-0.078
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha99980000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.661; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)