9rbq

Semliki Forest virus trimer 1 in complex with ApoER2 LA5

Method: ELECTRON MICROSCOPY Dmax: 191.7 Å Quality: REASONABLE

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

LDL receptor related protein 8,Ig gamma-2A chain C region, A allele

Mus musculus

UniProt E9PKG2

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 × 13 其他Polymer 9 PDB declaration: 13-meric(13) Consistent with protein copy count Chain A; UniProt 202–254 Not recorded Protein E3 × 3 (P0DJZ6) Structural polyprotein × 3 (A0A0F6PP03) Envelope glycoprotein E2 × 3 (P0DJZ6) Capsid protein × 3 (P0DJZ6) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name E9PKG2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–55; UniProt 202–254

LDL receptor related protein 8,Ig gamma-2A chain C region, A allele

Mus musculus

UniProt P01863

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 × 13 其他Polymer 9 PDB declaration: 13-meric(13) Consistent with protein copy count Chain A; UniProt 99–330 Not recorded Protein E3 × 3 (P0DJZ6) Structural polyprotein × 3 (A0A0F6PP03) Envelope glycoprotein E2 × 3 (P0DJZ6) Capsid protein × 3 (P0DJZ6) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCAA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 70–301; UniProt 99–330

Protein E3

Semliki Forest virus

UniProt P0DJZ6

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 × 13 其他Polymer 9 PDB declaration: 13-meric(13) Consistent with protein copy count Chain D; UniProt 268–333 Chain E; UniProt 268–333 Chain F; UniProt 268–333 Chain J; UniProt 334–755 Chain K; UniProt 334–755 Chain L; UniProt 334–755 Chain M; UniProt 1–267 Chain N; UniProt 1–267 Chain O; UniProt 1–267 Not recorded LDL receptor related protein 8,Ig gamma-2A chain C region, A allele × 1 (E9PKG2,P01863) Structural polyprotein × 3 (A0A0F6PP03) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLSF_SFV
Isoform
PDB entities 2, 4, 5
Chains and sequence ranges Author chain D; PDBConstruct 1–66; UniProt 268–333 Author chain E; PDBConstruct 1–66; UniProt 268–333 Author chain F; PDBConstruct 1–66; UniProt 268–333 Author chain J; PDBConstruct 1–422; UniProt 334–755 Author chain K; PDBConstruct 1–422; UniProt 334–755 Author chain L; PDBConstruct 1–422; UniProt 334–755 Author chain M; PDBConstruct 1–267; UniProt 1–267 Author chain N; PDBConstruct 1–267; UniProt 1–267 Author chain O; PDBConstruct 1–267; UniProt 1–267

Structural polyprotein

Semliki Forest virus

UniProt A0A0F6PP03

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 × 13 其他Polymer 9 PDB declaration: 13-meric(13) Consistent with protein copy count Chain G; UniProt 816–1253 Chain H; UniProt 816–1253 Chain I; UniProt 816–1253 Not recorded LDL receptor related protein 8,Ig gamma-2A chain C region, A allele × 1 (E9PKG2,P01863) Protein E3 × 3 (P0DJZ6) Envelope glycoprotein E2 × 3 (P0DJZ6) Capsid protein × 3 (P0DJZ6) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0F6PP03_SFV
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–438; UniProt 816–1253 Author chain H; PDBConstruct 1–438; UniProt 816–1253 Author chain I; PDBConstruct 1–438; UniProt 816–1253

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 9rbq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rbq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rbq
Deposition date deposition_date2025-05-27
Structure title titleSemliki Forest virus trimer 1 in complex with ApoER2 LA5
Keywords keywordsSemliki Forest virus, SFV, ApoER2 receptor, localized reconstruction, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.34
Radius of gyration Rg (electron density) rg_electron60.90
Forward intensity I(0) i01964590000.00
Molecular weight molecular_weight364950.0 kDa
Excluded volume excluded_volume453440 ų
Envelope volume envelope_volume755090 ų
Hydration-shell volume shell_volume103890 ų
Envelope diameter envelope_diameter190.5
Shell Rg shell_rg63.34
Envelope Rg envelope_rg58.79
Shape Rg shape_rg60.81
Total Rg total_rg61.25
Total atoms total_atoms25585
Residues n_residues3267
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 dmax191.7
Rg (real space) rg_real61.28
Rg uncertainty (real space) rg_real_error1.87
I(0) (real space) i0_real1.9650e+09
I(0) uncertainty (real space) i0_real_error4.0710e+07
Rg (reciprocal space) rg_reciprocal61.35
I(0) (reciprocal space) i0_reciprocal1965000000.0000
Solution quality estimate total_estimate0.6150
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.3
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76310000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)