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10dp

Human adenovirus hexon and polyclonal antibody complex

Method: ELECTRON MICROSCOPY Dmax: 141.4 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 3–958 Chain B； UniProt 3–958 Chain C； UniProt 3–958 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 3.25 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 10DP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
10DK Structure of an adenovirus hexon with Zwitterionic insertion in HVR5 Deposited 2026-01-13 Different construct Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 1–958（958 aa）
Chain B 1–958（958 aa）
Chain C 1–958（958 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 3.22 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 1–956； UniProt 3–958 Author chain B； PDBConstruct 1–956； UniProt 3–958 Author chain C； PDBConstruct 1–956； UniProt 3–958

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 10dp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id10dp
Deposition date deposition_date2026-01-13
Structure title titleHuman adenovirus hexon and polyclonal antibody complex
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_guinier44.23 Å
Radius of gyration Rg (electron density) rg_electron43.27 Å
Forward intensity I(0) i01478860000.00
Molecular weight molecular_weight313750.0 kDa
Excluded volume excluded_volume389830 ų
Envelope volume envelope_volume538840 ų
Hydration-shell volume shell_volume97369 ų
Envelope diameter envelope_diameter147.7 Å
Shell Rg shell_rg52.51 Å
Envelope Rg envelope_rg43.10 Å
Shape Rg shape_rg43.24 Å
Total Rg total_rg43.73 Å
Total atoms total_atoms22126
Residues n_residues2783
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 dmax141.4 Å
Rg (real space) rg_real43.98 Å
Rg uncertainty (real space) rg_real_error0.96 Å
I(0) (real space) i0_real1.4790e+09
I(0) uncertainty (real space) i0_real_error2.6990e+07
Rg (reciprocal space) rg_reciprocal44.23 Å
I(0) (reciprocal space) i0_reciprocal1479000000.0000
Solution quality estimate total_estimate0.8796
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.9 Å
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.375
Angular range angular_range— – 0.1800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha426600000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.906
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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)