9v55

Structure of TolC, YbjP, and AcrA complex

Method: ELECTRON MICROSCOPY Dmax: 214.7 Å Quality: GOOD

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

Outer membrane protein TolC

Escherichia coli K-12

UniProt P02930

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C1; UniProt 1–493 Chain C2; UniProt 1–493 Chain C3; UniProt 1–493 Not recorded Uncharacterized lipoprotein YbjP × 3 (P75818) Multidrug efflux pump subunit AcrA × 6 (P0AE06) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.26 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOLC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain C1; PDBConstruct 1–493; UniProt 1–493 Author chain C2; PDBConstruct 1–493; UniProt 1–493 Author chain C3; PDBConstruct 1–493; UniProt 1–493

Uncharacterized lipoprotein YbjP

Escherichia coli K-12

UniProt P75818

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain P1; UniProt 1–171 Chain P2; UniProt 1–171 Chain P3; UniProt 1–171 Not recorded Outer membrane protein TolC × 3 (P02930) Multidrug efflux pump subunit AcrA × 6 (P0AE06) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.26 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YBJP_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain P1; PDBConstruct 1–171; UniProt 1–171 Author chain P2; PDBConstruct 1–171; UniProt 1–171 Author chain P3; PDBConstruct 1–171; UniProt 1–171

Multidrug efflux pump subunit AcrA

Escherichia coli K-12

UniProt P0AE06

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A1; UniProt 1–397 Chain A2; UniProt 1–397 Chain A3; UniProt 1–397 Chain a1; UniProt 1–397 Chain a2; UniProt 1–397 Chain a3; UniProt 1–397 Not recorded Outer membrane protein TolC × 3 (P02930) Uncharacterized lipoprotein YbjP × 3 (P75818) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.26 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.

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

View Construct and Data Evidence
UniProt name ACRA_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain A1; PDBConstruct 1–397; UniProt 1–397 Author chain A2; PDBConstruct 1–397; UniProt 1–397 Author chain A3; PDBConstruct 1–397; UniProt 1–397 Author chain a1; PDBConstruct 1–397; UniProt 1–397 Author chain a2; PDBConstruct 1–397; UniProt 1–397 Author chain a3; PDBConstruct 1–397; UniProt 1–397

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 9v55

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v55
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v55
Deposition date deposition_date2025-05-25
Structure title titleStructure of TolC, YbjP, and AcrA complex
Keywords keywordsMultidrug efflux pump, TolC, YbjP, AcrA, AcrB, lipoprotein, antibiotic resistance, Gram-negative, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.62
Radius of gyration Rg (electron density) rg_electron80.73
Forward intensity I(0) i02503220000.00
Molecular weight molecular_weight412770.0 kDa
Excluded volume excluded_volume513830 ų
Envelope volume envelope_volume887490 ų
Hydration-shell volume shell_volume102210 ų
Envelope diameter envelope_diameter285.1
Shell Rg shell_rg61.62
Envelope Rg envelope_rg80.36
Shape Rg shape_rg80.67
Total Rg total_rg80.58
Total atoms total_atoms29061
Residues n_residues3816
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 dmax214.7
Rg (real space) rg_real75.64
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.4230e+09
I(0) uncertainty (real space) i0_real_error4.8790e+07
Rg (reciprocal space) rg_reciprocal76.18
I(0) (reciprocal space) i0_reciprocal2480000000.0000
Solution quality estimate total_estimate0.8621
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.4
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.816
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.1867
Highest regularization parameter α highest_alpha225900000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.845; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.008

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)