8ejd

Structure of lineage IV Lassa virus glycoprotein complex (strain Josiah)

Method: ELECTRON MICROSCOPY Dmax: 91.3 Å Quality: EXCELLENT

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

Glycoprotein G1

Lassa mammarenavirus

UniProt P08669

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 6 其他Polymer 27 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–259 Chain B; UniProt 1–259 Chain C; UniProt 1–259 Chain a; UniProt 260–424 Chain b; UniProt 260–424 Chain c; UniProt 260–424 Mutation:R207C, L258R, L259R Mutation:E329P, G360C beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;TBS cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 10 s; blotting time varied between 3-7 s; blotting force of 0 Resolution 3.80 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLYC_LASSJ
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–259; UniProt 1–259 Author chain B; PDBConstruct 1–259; UniProt 1–259 Author chain C; PDBConstruct 1–259; UniProt 1–259 Author chain a; PDBConstruct 1–165; UniProt 260–424 Author chain b; PDBConstruct 1–165; UniProt 260–424 Author chain c; PDBConstruct 1–165; UniProt 260–424

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 8ejd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ejd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ejd
Deposition date deposition_date2022-09-16
Structure title titleStructure of lineage IV Lassa virus glycoprotein complex (strain Josiah)
Keywords keywords;glycoprotein complex, Lassa mammarenavirus, LASV, GPC, immune system, viral fusion protein, Lassa virus, lineage IV, Josiah, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.01
Radius of gyration Rg (electron density) rg_electron30.72
Forward intensity I(0) i0329050000.00
Molecular weight molecular_weight140570.0 kDa
Excluded volume excluded_volume173880 ų
Envelope volume envelope_volume224020 ų
Hydration-shell volume shell_volume56447 ų
Envelope diameter envelope_diameter101.0
Shell Rg shell_rg40.68
Envelope Rg envelope_rg30.79
Shape Rg shape_rg30.69
Total Rg total_rg31.60
Total atoms total_atoms9804
Residues n_residues1086
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 dmax91.3
Rg (real space) rg_real31.71
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.2900e+08
I(0) uncertainty (real space) i0_real_error4.5170e+06
Rg (reciprocal space) rg_reciprocal31.84
I(0) (reciprocal space) i0_reciprocal329100000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.043
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha120900000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)