8t5c

Lassa GPC Trimer in complex with Fab 8.11G and nanobody D5

Method: ELECTRON MICROSCOPY Dmax: 125.8 Å Quality: GOOD

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

Glycoprotein G1

Lassa virus Josiah

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 × 11 其他Polymer 16 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 59–257 Chain B; UniProt 59–257 Chain C; UniProt 59–257 Chain a; UniProt 260–418 Chain b; UniProt 260–418 Chain c; UniProt 260–418 Not recorded D5 nanobody × 1 8.11G Heavy Chain × 2 8.11G Light Chain × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[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 ; × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-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 ; × 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 ; × 2 ;alpha-D-mannopyranose-(1-2)-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)]alpha-D-mannopyranose × 1 ;alpha-D-mannopyranose-(1-6)-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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 23 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;PBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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 1–200; UniProt 59–257 Author chain B; PDBConstruct 1–200; UniProt 59–257 Author chain C; PDBConstruct 1–200; UniProt 59–257 Author chain a; PDBConstruct 1–159; UniProt 260–418 Author chain b; PDBConstruct 1–159; UniProt 260–418 Author chain c; PDBConstruct 1–159; UniProt 260–418

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 8t5c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t5c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t5c
Deposition date deposition_date2023-06-13
Structure title titleLassa GPC Trimer in complex with Fab 8.11G and nanobody D5
Keywords keywordsvaccine, GPC, GP1, GP2, 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_guinier39.22
Radius of gyration Rg (electron density) rg_electron38.80
Forward intensity I(0) i0654488000.00
Molecular weight molecular_weight202740.0 kDa
Excluded volume excluded_volume250970 ų
Envelope volume envelope_volume335450 ų
Hydration-shell volume shell_volume70529 ų
Envelope diameter envelope_diameter137.0
Shell Rg shell_rg45.65
Envelope Rg envelope_rg38.73
Shape Rg shape_rg38.80
Total Rg total_rg39.16
Total atoms total_atoms14189
Residues n_residues1636
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 dmax125.8
Rg (real space) rg_real39.08
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real6.5450e+08
I(0) uncertainty (real space) i0_real_error9.9290e+06
Rg (reciprocal space) rg_reciprocal39.17
I(0) (reciprocal space) i0_reciprocal654500000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha253000000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)