9kn3

Cryo-EM structure of LptDEM complex from Escherichia coli

Method: ELECTRON MICROSCOPY Dmax: 117.2 Å Quality: REASONABLE

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

LPS-assembly protein LptD

Escherichia coli K-12

UniProt P31554

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 25–784 Not recorded LPS-assembly lipoprotein LptE × 1 (P0ADC1) Uncharacterized lipoprotein YifL × 1 (P0ADN6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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.

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

View Construct and Data Evidence
UniProt name LPTD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–760; UniProt 25–784

LPS-assembly lipoprotein LptE

Escherichia coli K-12

UniProt P0ADC1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 19–193 Not recorded LPS-assembly protein LptD × 1 (P31554) Uncharacterized lipoprotein YifL × 1 (P0ADN6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LPTE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–175; UniProt 19–193

Uncharacterized lipoprotein YifL

Escherichia coli K-12

UniProt P0ADN6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 20–67 Not recorded LPS-assembly protein LptD × 1 (P31554) LPS-assembly lipoprotein LptE × 1 (P0ADC1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YIFL_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–48; UniProt 20–67

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 9kn3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kn3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9kn3
Deposition date deposition_date2024-11-18
Structure title titleCryo-EM structure of LptDEM complex from Escherichia coli
Keywords keywordsLPS, Transporter, Complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.57
Radius of gyration Rg (electron density) rg_electron34.19
Forward intensity I(0) i0182592000.00
Molecular weight molecular_weight104760.0 kDa
Excluded volume excluded_volume129500 ų
Envelope volume envelope_volume175810 ų
Hydration-shell volume shell_volume44435 ų
Envelope diameter envelope_diameter124.9
Shell Rg shell_rg39.77
Envelope Rg envelope_rg33.80
Shape Rg shape_rg34.21
Total Rg total_rg34.57
Total atoms total_atoms7392
Residues n_residues917
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 dmax117.2
Rg (real space) rg_real34.71
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.8260e+08
I(0) uncertainty (real space) i0_real_error2.8510e+06
Rg (reciprocal space) rg_reciprocal34.62
I(0) (reciprocal space) i0_reciprocal182600000.0000
Solution quality estimate total_estimate0.6618
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21240000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.122; Positv: 1.000; Valcen: 0.980; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)