8tye

Lassa GPC (strain Josiah) bound to rabbit polyclonal fusion-peptide-targeting antibody FP-1

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: GOOD

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

Glycoprotein GP1

Lassa virus (strain Mouse/Sierra Leone/Josiah/1976)

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 Insufficient information 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 Not recorded Polyclonal Fv heavy chain × 1 Polyclonal Fv light chain × 1 alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;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)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 11 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 × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE 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 3, 4
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

Glycoprotein GP2

Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

UniProt Q9WXS1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 其他Polymer 19 PDB declaration: octameric(8) Consistent with protein copy count Chain a; UniProt 2–205 Chain b; UniProt 2–205 Chain c; UniProt 2–205 Not recorded Polyclonal Fv heavy chain × 1 Polyclonal Fv light chain × 1 Glycoprotein GP1 × 3 (P08669) alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;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)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 11 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 × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE 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.

16 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WXS1_THEMA
Isoform
PDB entities 4
Chains and sequence ranges Author chain a; PDBConstruct 191–394; UniProt 2–205 Author chain b; PDBConstruct 191–394; UniProt 2–205 Author chain c; PDBConstruct 191–394; UniProt 2–205

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 8tye

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tye
Deposition date deposition_date2023-08-25
Structure title titleLassa GPC (strain Josiah) bound to rabbit polyclonal fusion-peptide-targeting antibody FP-1
Keywords keywords;Lassa virus glycoprotein complex, GPC, immune complex, antibody, polyclonal antibody, base antibody, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex ;; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.03
Radius of gyration Rg (electron density) rg_electron32.82
Forward intensity I(0) i0338272000.00
Molecular weight molecular_weight141860.0 kDa
Excluded volume excluded_volume174900 ų
Envelope volume envelope_volume234490 ų
Hydration-shell volume shell_volume56753 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg41.34
Envelope Rg envelope_rg33.50
Shape Rg shape_rg32.88
Total Rg total_rg33.25
Total atoms total_atoms9921
Residues n_residues1205
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 dmax108.8
Rg (real space) rg_real33.94
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real3.3830e+08
I(0) uncertainty (real space) i0_real_error5.0120e+06
Rg (reciprocal space) rg_reciprocal33.99
I(0) (reciprocal space) i0_reciprocal338300000.0000
Solution quality estimate total_estimate0.8735
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.7
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.174
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha133300000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.782

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)