13hs

Cryo-EM structure of Pseudomonas aeruginosa outer-membrane lipoprotein PA3214 in the open conformation

Method: ELECTRON MICROSCOPY Dmax: 122.9 Å Quality: GOOD

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

ABC-type transport auxiliary lipoprotein component domain-containing protein

Pseudomonas aeruginosa PAO1

UniProt Q9HZ26

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 homooligomer Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–214 Chain B; UniProt 1–214 Chain C; UniProt 1–214 Chain D; UniProt 1–214 Chain E; UniProt 1–214 Chain F; UniProt 1–214 Chain G; UniProt 1–214 Chain H; UniProt 1–214 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9HZ26_PSEAE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–214; UniProt 1–214 Author chain B; PDBConstruct 1–214; UniProt 1–214 Author chain C; PDBConstruct 1–214; UniProt 1–214 Author chain D; PDBConstruct 1–214; UniProt 1–214 Author chain E; PDBConstruct 1–214; UniProt 1–214 Author chain F; PDBConstruct 1–214; UniProt 1–214 Author chain G; PDBConstruct 1–214; UniProt 1–214 Author chain H; PDBConstruct 1–214; UniProt 1–214

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 13hs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 13hs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id13hs
Deposition date deposition_date2026-05-06
Structure title titleCryo-EM structure of Pseudomonas aeruginosa outer-membrane lipoprotein PA3214 in the open conformation
Keywords keywordsouter membrane lipoprotein, Pseudomonas aeruginosa, MCE system, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.41
Radius of gyration Rg (electron density) rg_electron41.61
Forward intensity I(0) i0385847000.00
Molecular weight molecular_weight156260.0 kDa
Excluded volume excluded_volume194190 ų
Envelope volume envelope_volume311970 ų
Hydration-shell volume shell_volume60649 ų
Envelope diameter envelope_diameter122.3
Shell Rg shell_rg50.53
Envelope Rg envelope_rg38.98
Shape Rg shape_rg41.63
Total Rg total_rg42.05
Total atoms total_atoms11040
Residues n_residues1424
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 dmax122.9
Rg (real space) rg_real42.14
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real3.8580e+08
I(0) uncertainty (real space) i0_real_error6.1270e+06
Rg (reciprocal space) rg_reciprocal42.41
I(0) (reciprocal space) i0_reciprocal386000000.0000
Solution quality estimate total_estimate0.8870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.8
Skewness Skewness skewness-0.143
Kurtosis Kurtosis kurtosis-0.886
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85880000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)