8zar

EmrAB-TolC MFS-type tripartite multidrug efflux pump FA

Method: ELECTRON MICROSCOPY Dmax: 229.5 Å Quality: GOOD

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

Multidrug export protein EmrA

Escherichia coli K-12

UniProt P27303

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–390 Chain B; UniProt 1–390 Chain C; UniProt 1–390 Chain D; UniProt 1–390 Chain E; UniProt 1–390 Chain F; UniProt 1–390 Not recorded Multidrug export protein EmrB × 1 (P0AEJ0) Outer membrane protein TolC × 3 (P02930) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 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 EMRA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–390; UniProt 1–390 Author chain B; PDBConstruct 1–390; UniProt 1–390 Author chain C; PDBConstruct 1–390; UniProt 1–390 Author chain D; PDBConstruct 1–390; UniProt 1–390 Author chain E; PDBConstruct 1–390; UniProt 1–390 Author chain F; PDBConstruct 1–390; UniProt 1–390

Multidrug export protein EmrB

Escherichia coli K-12

UniProt P0AEJ0

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain J; UniProt 10–503 Not recorded Multidrug export protein EmrA × 6 (P27303) Outer membrane protein TolC × 3 (P02930) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 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 EMRB_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 121–614; UniProt 10–503

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–493 Chain H; UniProt 1–493 Chain I; UniProt 1–493 Mutation:V191L Multidrug export protein EmrA × 6 (P27303) Multidrug export protein EmrB × 1 (P0AEJ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–493; UniProt 1–493 Author chain H; PDBConstruct 1–493; UniProt 1–493 Author chain I; PDBConstruct 1–493; UniProt 1–493

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 8zar

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zar
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zar
Deposition date deposition_date2024-04-25
Structure title titleEmrAB-TolC MFS-type tripartite multidrug efflux pump FA
Keywords keywordsMultidrug efflux pump, MFS, EmrAB, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier84.19
Radius of gyration Rg (electron density) rg_electron86.56
Forward intensity I(0) i02577150000.00
Molecular weight molecular_weight424530.0 kDa
Excluded volume excluded_volume530810 ų
Envelope volume envelope_volume875850 ų
Hydration-shell volume shell_volume100810 ų
Envelope diameter envelope_diameter324.2
Shell Rg shell_rg59.83
Envelope Rg envelope_rg85.80
Shape Rg shape_rg86.61
Total Rg total_rg85.92
Total atoms total_atoms29869
Residues n_residues3880
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 dmax229.5
Rg (real space) rg_real77.51
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.4670e+09
I(0) uncertainty (real space) i0_real_error4.8660e+07
Rg (reciprocal space) rg_reciprocal77.34
I(0) (reciprocal space) i0_reciprocal2528000000.0000
Solution quality estimate total_estimate0.7875
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.508
Kurtosis Kurtosis kurtosis-0.799
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.1883
Highest regularization parameter α highest_alpha366200000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.508; Stabil: 0.974; Sysdev: 1.000; Positv: 1.000; Valcen: 0.772; Smooth: 0.023

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)