7fdj

Engineered Hepatitis B virus core antigen with short linker T=4

Method: ELECTRON MICROSCOPY Dmax: 100.2 Å Quality: GOOD

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

Capsid protein,Immunoglobulin G-binding protein A

Hepatitis B virus genotype C subtype adr (strain Japan/adr4/1983)

UniProt P38507

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 Homooligomer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain A; UniProt 212–269 Chain A; UniProt 212–269 Chain B; UniProt 212–269 Chain B; UniProt 212–269 Chain C; UniProt 212–269 Chain C; UniProt 212–269 Chain D; UniProt 212–269 Chain D; UniProt 212–269 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
2 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 212–269 Chain A; UniProt 212–269 Chain B; UniProt 212–269 Chain B; UniProt 212–269 Chain C; UniProt 212–269 Chain C; UniProt 212–269 Chain D; UniProt 212–269 Chain D; UniProt 212–269 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
3 Insufficient information Homooligomer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain A; UniProt 212–269 Chain A; UniProt 212–269 Chain B; UniProt 212–269 Chain B; UniProt 212–269 Chain C; UniProt 212–269 Chain C; UniProt 212–269 Chain D; UniProt 212–269 Chain D; UniProt 212–269 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
4 Insufficient information Homooligomer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 212–269 Chain A; UniProt 212–269 Chain B; UniProt 212–269 Chain B; UniProt 212–269 Chain C; UniProt 212–269 Chain C; UniProt 212–269 Chain D; UniProt 212–269 Chain D; UniProt 212–269 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
5 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 212–269 Chain A; UniProt 212–269 Chain B; UniProt 212–269 Chain B; UniProt 212–269 Chain C; UniProt 212–269 Chain C; UniProt 212–269 Chain D; UniProt 212–269 Chain D; UniProt 212–269 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

66 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 130–187; UniProt 212–269 Author chain A; PDBConstruct 190–247; UniProt 212–269 Author chain B; PDBConstruct 130–187; UniProt 212–269 Author chain B; PDBConstruct 190–247; UniProt 212–269 Author chain C; PDBConstruct 130–187; UniProt 212–269 Author chain C; PDBConstruct 190–247; UniProt 212–269 Author chain D; PDBConstruct 130–187; UniProt 212–269 Author chain D; PDBConstruct 190–247; UniProt 212–269

Capsid protein,Immunoglobulin G-binding protein A

Hepatitis B virus genotype C subtype adr (strain Japan/adr4/1983)

UniProt P69706

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 Homooligomer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain A; UniProt 2–78 Chain A; UniProt 81–149 Chain B; UniProt 2–78 Chain B; UniProt 81–149 Chain C; UniProt 2–78 Chain C; UniProt 81–149 Chain D; UniProt 2–78 Chain D; UniProt 81–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
2 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–78 Chain A; UniProt 81–149 Chain B; UniProt 2–78 Chain B; UniProt 81–149 Chain C; UniProt 2–78 Chain C; UniProt 81–149 Chain D; UniProt 2–78 Chain D; UniProt 81–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
3 Insufficient information Homooligomer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain A; UniProt 2–78 Chain A; UniProt 81–149 Chain B; UniProt 2–78 Chain B; UniProt 81–149 Chain C; UniProt 2–78 Chain C; UniProt 81–149 Chain D; UniProt 2–78 Chain D; UniProt 81–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
4 Insufficient information Homooligomer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 2–78 Chain A; UniProt 81–149 Chain B; UniProt 2–78 Chain B; UniProt 81–149 Chain C; UniProt 2–78 Chain C; UniProt 81–149 Chain D; UniProt 2–78 Chain D; UniProt 81–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
5 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–78 Chain A; UniProt 81–149 Chain B; UniProt 2–78 Chain B; UniProt 81–149 Chain C; UniProt 2–78 Chain C; UniProt 81–149 Chain D; UniProt 2–78 Chain D; UniProt 81–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPSD_HBVC3
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 51–127; UniProt 2–78 Author chain A; PDBConstruct 250–318; UniProt 81–149 Author chain B; PDBConstruct 51–127; UniProt 2–78 Author chain B; PDBConstruct 250–318; UniProt 81–149 Author chain C; PDBConstruct 51–127; UniProt 2–78 Author chain C; PDBConstruct 250–318; UniProt 81–149 Author chain D; PDBConstruct 51–127; UniProt 2–78 Author chain D; PDBConstruct 250–318; UniProt 81–149

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 7fdj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7fdj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7fdj
Deposition date deposition_date2021-07-16
Structure title titleEngineered Hepatitis B virus core antigen with short linker T=4
Keywords keywordscancer therapy, epidermal growth factor receptor 1, affibody, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.09
Radius of gyration Rg (electron density) rg_electron30.71
Forward intensity I(0) i057104600.00
Molecular weight molecular_weight62404.0 kDa
Excluded volume excluded_volume79327 ų
Envelope volume envelope_volume108740 ų
Hydration-shell volume shell_volume30001 ų
Envelope diameter envelope_diameter105.8
Shell Rg shell_rg36.92
Envelope Rg envelope_rg30.50
Shape Rg shape_rg30.74
Total Rg total_rg31.25
Total atoms total_atoms4416
Residues n_residues548
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 dmax100.2
Rg (real space) rg_real31.14
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real5.7100e+07
I(0) uncertainty (real space) i0_real_error9.8100e+05
Rg (reciprocal space) rg_reciprocal31.12
I(0) (reciprocal space) i0_reciprocal57100000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18000000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)