9rlj

LolCDE with bound ATPgammaS

Method: ELECTRON MICROSCOPY Dmax: 133.2 Å Quality: REASONABLE

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

Lipoprotein-releasing system transmembrane protein LolC

Escherichia coli K-12

UniProt P0ADC3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–399 Not recorded Lipoprotein-releasing system transmembrane protein LolE × 1 (P75958) Lipoprotein-releasing system ATP-binding protein LolD × 2 (P75957) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

18 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–399; UniProt 1–399

Lipoprotein-releasing system transmembrane protein LolE

Escherichia coli K-12

UniProt P75958

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–414 Not recorded Lipoprotein-releasing system transmembrane protein LolC × 1 (P0ADC3) Lipoprotein-releasing system ATP-binding protein LolD × 2 (P75957) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–414; UniProt 1–414

Lipoprotein-releasing system ATP-binding protein LolD

Escherichia coli K-12

UniProt P75957

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–233 Chain F; UniProt 1–233 Mutation:C-terminal His tag (GSHHHHHH) Lipoprotein-releasing system transmembrane protein LolC × 1 (P0ADC3) Lipoprotein-releasing system transmembrane protein LolE × 1 (P75958) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLD_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–233; UniProt 1–233 Author chain F; PDBConstruct 1–233; UniProt 1–233

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 9rlj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rlj
Deposition date deposition_date2025-06-16
Structure title titleLolCDE with bound ATPgammaS
Keywords keywordsGram-negative, envelope biogenesis, outer membrane protein, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.53
Radius of gyration Rg (electron density) rg_electron44.23
Forward intensity I(0) i0279660000.00
Molecular weight molecular_weight139370.0 kDa
Excluded volume excluded_volume175640 ų
Envelope volume envelope_volume240320 ų
Hydration-shell volume shell_volume47709 ų
Envelope diameter envelope_diameter142.6
Shell Rg shell_rg45.80
Envelope Rg envelope_rg43.76
Shape Rg shape_rg44.24
Total Rg total_rg44.29
Total atoms total_atoms9775
Residues n_residues1268
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 dmax133.2
Rg (real space) rg_real44.97
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real2.7970e+08
I(0) uncertainty (real space) i0_real_error4.8740e+06
Rg (reciprocal space) rg_reciprocal44.53
I(0) (reciprocal space) i0_reciprocal279500000.0000
Solution quality estimate total_estimate0.7327
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.913
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74100000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.625; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.653; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)