6suf

Structure of Photorhabdus luminescens Tc holotoxin pore

Method: ELECTRON MICROSCOPY Dmax: 209.4 Å Quality: EXCELLENT

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

TcdA1

Photorhabdus luminescens

UniProt Q9RN43

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 1–2516 Chain B; UniProt 1–2516 Chain C; UniProt 1–2516 Chain D; UniProt 1–2516 Chain E; UniProt 1–2516 Not recorded TcdB2,TccC3 × 1 (Q8GF99,Q8GF97) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9RN43_PHOLU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2516; UniProt 1–2516 Author chain B; PDBConstruct 1–2516; UniProt 1–2516 Author chain C; PDBConstruct 1–2516; UniProt 1–2516 Author chain D; PDBConstruct 1–2516; UniProt 1–2516 Author chain E; PDBConstruct 1–2516; UniProt 1–2516

TcdB2,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 1–960 Not recorded TcdA1 × 5 (Q9RN43) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1480–2439; UniProt 1–960

TcdB2,TccC3

Photorhabdus luminescens

UniProt Q8GF99

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 1–1474 Not recorded TcdA1 × 5 (Q9RN43) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8GF99_PHOLU
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–1474; UniProt 1–1474

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 6suf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6suf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6suf
Deposition date deposition_date2019-09-13
Structure title titleStructure of Photorhabdus luminescens Tc holotoxin pore
Keywords keywordsComplex, Holotoxin, Photorhabdus, Insecticidal, Translocation, TOXIN; TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.98
Radius of gyration Rg (electron density) rg_electron82.49
Forward intensity I(0) i032479400000.00
Molecular weight molecular_weight1531900.0 kDa
Excluded volume excluded_volume1912900 ų
Envelope volume envelope_volume3033300 ų
Hydration-shell volume shell_volume297510 ų
Envelope diameter envelope_diameter355.2
Shell Rg shell_rg89.77
Envelope Rg envelope_rg81.17
Shape Rg shape_rg82.49
Total Rg total_rg82.54
Total atoms total_atoms108112
Residues n_residues13607
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 dmax209.4
Rg (real space) rg_real78.12
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.0930e+10
I(0) uncertainty (real space) i0_real_error5.4550e+08
Rg (reciprocal space) rg_reciprocal82.92
I(0) (reciprocal space) i0_reciprocal32480000000.0000
Solution quality estimate total_estimate0.9120
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary99.2
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.2594
Highest regularization parameter α highest_alpha6144000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.992; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)