6eqc

Cryo-EM reconstruction of a complex of a binding protein and human adenovirus C5 hexon

Method: ELECTRON MICROSCOPY Dmax: 177.1 Å Quality: REASONABLE

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

Hexon protein

OrganismNot specified

UniProt P04133

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–952 Chain B; UniProt 1–952 Chain C; UniProt 1–952 Not recorded scFv of 9C12 antibody × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 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.

11 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPSH_ADE05
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–952; UniProt 1–952 Author chain B; PDBConstruct 1–952; UniProt 1–952 Author chain C; PDBConstruct 1–952; UniProt 1–952

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 6eqc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6eqc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6eqc
Deposition date deposition_date2017-10-12
Structure title titleCryo-EM reconstruction of a complex of a binding protein and human adenovirus C5 hexon
Keywords keywordsAntibody, Human Adenovirus C5, gene therapy Viral Protein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.09
Radius of gyration Rg (electron density) rg_electron51.91
Forward intensity I(0) i02223420000.00
Molecular weight molecular_weight390130.0 kDa
Excluded volume excluded_volume485780 ų
Envelope volume envelope_volume677110 ų
Hydration-shell volume shell_volume107270 ų
Envelope diameter envelope_diameter179.4
Shell Rg shell_rg55.64
Envelope Rg envelope_rg52.13
Shape Rg shape_rg51.87
Total Rg total_rg52.14
Total atoms total_atoms53964
Residues n_residues3462
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 dmax177.1
Rg (real space) rg_real52.05
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real2.2230e+09
I(0) uncertainty (real space) i0_real_error4.3440e+07
Rg (reciprocal space) rg_reciprocal52.11
I(0) (reciprocal space) i0_reciprocal2224000000.0000
Solution quality estimate total_estimate0.6522
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.9
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha212600000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.987; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)