9ia5

LpDEM from Escherichia coli

Method: ELECTRON MICROSCOPY Dmax: 114.0 Å Quality: GOOD

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

LPS-assembly protein LptD

Escherichia coli

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 1–784 Not recorded LPS-assembly lipoprotein LptE × 1 (P0ADC1) LPS-assembly lipoprotein LptM × 1 (P0ADN6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.63 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 1–784; UniProt 1–784

LPS-assembly lipoprotein LptE

Escherichia coli

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 1–193 Not recorded LPS-assembly protein LptD × 1 (P31554) LPS-assembly lipoprotein LptM × 1 (P0ADN6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.63 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 1–193; UniProt 1–193

LPS-assembly lipoprotein LptM

Escherichia coli

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 D; UniProt 1–67 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 2.63 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 LPTM_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–67; UniProt 1–67

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 9ia5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ia5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ia5
Deposition date deposition_date2025-02-07
最后修订 last_revision2025-12-10
Structure title titleLpDEM from Escherichia coli
Keywords keywordsLipopolysaccharide transport, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.53
Radius of gyration Rg (electron density) rg_electron33.06
Forward intensity I(0) i0172796000.00
Molecular weight molecular_weight102080.0 kDa
Excluded volume excluded_volume126360 ų
Envelope volume envelope_volume171340 ų
Hydration-shell volume shell_volume44204 ų
Envelope diameter envelope_diameter121.8
Shell Rg shell_rg39.39
Envelope Rg envelope_rg32.74
Shape Rg shape_rg33.05
Total Rg total_rg33.55
Total atoms total_atoms14061
Residues n_residues891
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 dmax114.0
Rg (real space) rg_real33.60
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.7280e+08
I(0) uncertainty (real space) i0_real_error2.7770e+06
Rg (reciprocal space) rg_reciprocal33.55
I(0) (reciprocal space) i0_reciprocal172800000.0000
Solution quality estimate total_estimate0.8694
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary111.5
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.164
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21980000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)