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10dk

Structure of an adenovirus hexon with Zwitterionic insertion in HVR5

Method: ELECTRON MICROSCOPY Dmax: 139.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Hexon protein

Human adenovirus 57

UniProt A0A348FV85

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 1–958 Chain B； UniProt 1–958 Chain C； UniProt 1–958 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；20mM HEPES pH 7.2 300 mM NaCl cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.22 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.

Other PDB Difference from Current Entry 10DK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
10DP Human adenovirus hexon and polyclonal antibody complex Deposited 2026-01-13 Different construct Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 3–958（956 aa）
Chain B 3–958（956 aa）
Chain C 3–958（956 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2；20mM HEPES pH 7.2 300 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.25 Å
9CM9 Cryo-EM model derived from localized reconstruction of Ad657-hexon-FX complex at 3.86A resolution Deposited 2024-07-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 1–959（959 aa）
Chain K 1–959（959 aa）
Chain L 1–959（959 aa）
Not recorded CA CALCIUM ION × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
9CMO Cryo-EM model derived from localized reconstruction of Ad657-hexon-FII complex at 4.14A resolution Deposited 2024-07-15 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 1–959（959 aa）
Chain K 1–959（959 aa）
Chain L 1–959（959 aa）
Not recorded CA CALCIUM ION × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.17 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A348FV85_9ADEN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–926； UniProt 1–958 Author chain B； PDBConstruct 1–926； UniProt 1–958 Author chain C； PDBConstruct 1–926； UniProt 1–958

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 10dk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10dk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10dk
Deposition date deposition_date2026-01-13
Structure title titleStructure of an adenovirus hexon with Zwitterionic insertion in HVR5
Keywords keywords;Viral vectors, capsid engineering, zwitterionic peptides, adenoviruses, immune stealth, blood factors, neutralizing antibodies, cryo-EM, VIRUS, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier43.86 Å
Radius of gyration Rg (electron density) rg_electron42.89 Å
Forward intensity I(0) i01456700000.00
Molecular weight molecular_weight311430.0 kDa
Excluded volume excluded_volume386970 ų
Envelope volume envelope_volume526920 ų
Hydration-shell volume shell_volume96074 ų
Envelope diameter envelope_diameter146.9 Å
Shell Rg shell_rg52.21 Å
Envelope Rg envelope_rg42.64 Å
Shape Rg shape_rg42.87 Å
Total Rg total_rg43.35 Å
Total atoms total_atoms21963
Residues n_residues2764
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax139.4 Å
Rg (real space) rg_real43.61 Å
Rg uncertainty (real space) rg_real_error0.92 Å
I(0) (real space) i0_real1.4570e+09
I(0) uncertainty (real space) i0_real_error2.6010e+07
Rg (reciprocal space) rg_reciprocal43.86 Å
I(0) (reciprocal space) i0_reciprocal1457000000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.1 Å
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.1800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha428000000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.904
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)