8eji

Lassa virus glycoprotein complex (Josiah) bound to 19.7E Fab

Method: ELECTRON MICROSCOPY Dmax: 116.3 Å Quality: REASONABLE

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 Heteromer Protein × 8 其他Polymer 19 PDB declaration: octameric(8) 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:E328P, G359C 19.7E Fab heavy chain × 1 19.7E Fab light chain × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;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 ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-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 ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 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 3.81 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 8eji

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8eji
Deposition date deposition_date2022-09-16
Structure title titleLassa virus glycoprotein complex (Josiah) bound to 19.7E Fab
Keywords keywords;glycoprotein complex, Lassa mammarenavirus, LASV, GPC, immune system, viral fusion protein, Lassa virus, lineage IV, Josiah, 19.7E, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.52
Radius of gyration Rg (electron density) rg_electron34.92
Forward intensity I(0) i0398339000.00
Molecular weight molecular_weight157780.0 kDa
Excluded volume excluded_volume195760 ų
Envelope volume envelope_volume253160 ų
Hydration-shell volume shell_volume58864 ų
Envelope diameter envelope_diameter122.7
Shell Rg shell_rg42.51
Envelope Rg envelope_rg35.20
Shape Rg shape_rg34.92
Total Rg total_rg35.44
Total atoms total_atoms11023
Residues n_residues1257
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 dmax116.3
Rg (real space) rg_real36.29
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.9340e+08
I(0) uncertainty (real space) i0_real_error5.5050e+06
Rg (reciprocal space) rg_reciprocal35.51
I(0) (reciprocal space) i0_reciprocal398300000.0000
Solution quality estimate total_estimate0.6987
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.4
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha2.9060
Highest regularization parameter α highest_alpha149500000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 0.922; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.746

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8ejiH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8ejiL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)