5lid

X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) in complex with bromopromazine

Method: X-RAY DIFFRACTION Dmax: 162.3 Å Quality: GOOD

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

Cys-loop ligand-gated ion channel

Dickeya chrysanthemi

UniProt P0C7B7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 11–316 Chain B; UniProt 11–316 Chain C; UniProt 11–316 Chain D; UniProt 11–316 Chain E; UniProt 11–316 Not recorded 6XY bromopromazine × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;200 mM ammonium sulfate, 50 mM ADA pH 6.5, 9-12 % PEG4000 Resolution 4.50 Å R-free 0.257
2 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 11–316 Chain G; UniProt 11–316 Chain H; UniProt 11–316 Chain I; UniProt 11–316 Chain J; UniProt 11–316 Not recorded 6XY bromopromazine × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;200 mM ammonium sulfate, 50 mM ADA pH 6.5, 9-12 % PEG4000 Resolution 4.50 Å R-free 0.257

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.

17 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELIC_DICCH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–307; UniProt 11–316 Author chain B; PDBConstruct 1–307; UniProt 11–316 Author chain C; PDBConstruct 1–307; UniProt 11–316 Author chain D; PDBConstruct 1–307; UniProt 11–316 Author chain E; PDBConstruct 1–307; UniProt 11–316 Author chain F; PDBConstruct 1–307; UniProt 11–316 Author chain G; PDBConstruct 1–307; UniProt 11–316 Author chain H; PDBConstruct 1–307; UniProt 11–316 Author chain I; PDBConstruct 1–307; UniProt 11–316 Author chain J; PDBConstruct 1–307; UniProt 11–316

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 5lid

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lid
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5lid
Deposition date deposition_date2016-07-14
Structure title titleX-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) in complex with bromopromazine
Keywords keywordsligand-gated ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier51.93
Radius of gyration Rg (electron density) rg_electron51.51
Forward intensity I(0) i01638490000.00
Molecular weight molecular_weight354910.0 kDa
Excluded volume excluded_volume449810 ų
Envelope volume envelope_volume637600 ų
Hydration-shell volume shell_volume99945 ų
Envelope diameter envelope_diameter161.9
Shell Rg shell_rg57.39
Envelope Rg envelope_rg50.38
Shape Rg shape_rg51.51
Total Rg total_rg51.70
Total atoms total_atoms25070
Residues n_residues3070
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 dmax162.3
Rg (real space) rg_real51.82
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real1.6380e+09
I(0) uncertainty (real space) i0_real_error2.9630e+07
Rg (reciprocal space) rg_reciprocal52.00
I(0) (reciprocal space) i0_reciprocal1639000000.0000
Solution quality estimate total_estimate0.8354
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.1
Skewness Skewness skewness0.185
Kurtosis Kurtosis kurtosis-0.688
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha366200000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)