SAXSdb — 3tg7

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

Hexon protein

OrganismNot specified

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 2–952	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；14% PEG 6000 in Bis-tris propane buffer., pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.57 Å R-free 0.223

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 3TG7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1P30 Refinement of Adenovirus Type 5 Hexon with CNS Deposited 2003-04-16	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–951（951 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.2；298 K；0.5 SODIUM CITRATE , pH 3.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.207
4V4U The quasi-atomic model of Human Adenovirus type 5 capsid Deposited 2005-03-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 840 PDB declaration: 840-meric	Chain F 1–951（951 aa） Chain G 1–951（951 aa） Chain H 1–951（951 aa） Chain I 1–951（951 aa） Chain J 1–951（951 aa） Chain K 1–951（951 aa） Chain L 1–951（951 aa） Chain M 1–951（951 aa） Chain N 1–951（951 aa） Chain O 1–951（951 aa） Chain P 1–951（951 aa） Chain Q 1–951（951 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.5；TRIS cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 10.00 Å
4V4U The quasi-atomic model of Human Adenovirus type 5 capsid Deposited 2005-03-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain F 1–951（951 aa） Chain G 1–951（951 aa） Chain H 1–951（951 aa） Chain I 1–951（951 aa） Chain J 1–951（951 aa） Chain K 1–951（951 aa） Chain L 1–951（951 aa） Chain M 1–951（951 aa） Chain N 1–951（951 aa） Chain O 1–951（951 aa） Chain P 1–951（951 aa） Chain Q 1–951（951 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.5；TRIS cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 10.00 Å
4V4U The quasi-atomic model of Human Adenovirus type 5 capsid Deposited 2005-03-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain F 1–951（951 aa） Chain G 1–951（951 aa） Chain H 1–951（951 aa） Chain I 1–951（951 aa） Chain J 1–951（951 aa） Chain K 1–951（951 aa） Chain L 1–951（951 aa） Chain M 1–951（951 aa） Chain N 1–951（951 aa） Chain O 1–951（951 aa） Chain P 1–951（951 aa） Chain Q 1–951（951 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.5；TRIS cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 10.00 Å
5LDN A viral capsid:antibody complex Deposited 2016-06-27	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 8–947（940 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 4000, sodium chloride,	Resolution 2.70 Å R-free 0.223
5OGI Complex of a binding protein and human adenovirus C 5 hexon Deposited 2017-07-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–952（952 aa）	Not recorded	SO4 SULFATE ION × 7 DIO 1,4-DIETHYLENE DIOXIDE × 10 EDO 1,2-ETHANEDIOL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M (NH4)2SO4, 10 % dioxane, 0.1 M MES pH 6.5	Resolution 2.80 Å R-free 0.235
6B1T Improved cryoEM structure of human adenovirus type 5 with atomic details of minor proteins VI and VII Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1500 PDB declaration: 1500-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6B1T Improved cryoEM structure of human adenovirus type 5 with atomic details of minor proteins VI and VII Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6B1T Improved cryoEM structure of human adenovirus type 5 with atomic details of minor proteins VI and VII Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 125 PDB declaration: 125-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6B1T Improved cryoEM structure of human adenovirus type 5 with atomic details of minor proteins VI and VII Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 150 PDB declaration: 150-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6B1T Improved cryoEM structure of human adenovirus type 5 with atomic details of minor proteins VI and VII Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1260 PDB declaration: 1260-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 105 PDB declaration: 105-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 126 PDB declaration: 126-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6CGV Revised crystal structure of human adenovirus Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 1260 PDB declaration: 1260-meric	Chain A 4–952（949 aa） Chain B 4–952（949 aa） Chain C 4–952（949 aa） Chain D 4–952（949 aa） Chain E 4–952（949 aa） Chain F 4–952（949 aa） Chain G 4–952（949 aa） Chain H 4–952（949 aa） Chain I 4–952（949 aa） Chain J 4–952（949 aa） Chain K 4–952（949 aa） Chain L 4–952（949 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；100MM HEPES PH 7.0, 200MM CALCIUM ACETATE, 14% PEG550 MME, 15% GLYCEROL.	Resolution 3.80 Å R-free 0.427
6EQC Cryo-EM reconstruction of a complex of a binding protein and human adenovirus C5 hexon Deposited 2017-10-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.40 Å
7S78 Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation Deposited 2021-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1860 PDB declaration: 1860-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.1；40 mM Tris, pH 8.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
7S78 Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation Deposited 2021-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 31 PDB declaration: 31-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.1；40 mM Tris, pH 8.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
7S78 Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation Deposited 2021-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 155 PDB declaration: 155-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.1；40 mM Tris, pH 8.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
7S78 Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation Deposited 2021-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 186 PDB declaration: 186-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.1；40 mM Tris, pH 8.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
7S78 Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation Deposited 2021-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 31 PDB declaration: 31-meric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa） Chain D 1–952（952 aa） Chain E 1–952（952 aa） Chain F 1–952（952 aa） Chain G 1–952（952 aa） Chain H 1–952（952 aa） Chain I 1–952（952 aa） Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.1；40 mM Tris, pH 8.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
8Q7C Cryo-EM structure of Adenovirus C5 hexon Deposited 2023-08-16	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–952（952 aa） Chain B 1–952（952 aa） Chain C 1–952（952 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9CLI Cryo-EM model derived from localized reconstruction of human adenovirus (Ad5)-hexon-FX complex at 3.6A resolution Deposited 2024-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.61 Å
9CLN Cryo-EM model derived from localized reconstruction of human adenovirus 5 (Ad5)-hexon-FII complex at 3.9A resolution Deposited 2024-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 1–952（952 aa） Chain K 1–952（952 aa） Chain L 1–952（952 aa）	Not recorded	CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.13 Å

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

View Construct and Data Evidence

UniProt name	HEX_ADE05
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–951； UniProt 2–952

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3tg7
Deposition date deposition_date	2011-08-17
Structure title title	Crystal structure of Adenovirus serotype 5 hexon at 1.6A resolution
Keywords keywords	Adenovirus structural protein, with new finding featuring possible binding to human coagulation factor X, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	36.51 Å
Radius of gyration Rg (electron density) rg_electron	36.25 Å
Forward intensity I(0) i0	158019000.00
Molecular weight molecular_weight	100650.0 kDa
Excluded volume excluded_volume	125650 Å³
Envelope volume envelope_volume	181860 Å³
Hydration-shell volume shell_volume	42840 Å³
Envelope diameter envelope_diameter	130.0 Å
Shell Rg shell_rg	40.96 Å
Envelope Rg envelope_rg	37.31 Å
Shape Rg shape_rg	36.25 Å
Total Rg total_rg	36.61 Å
Total atoms total_atoms	7107
Residues n_residues	889
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	123.2 Å
Rg (real space) rg_real	36.67 Å
Rg uncertainty (real space) rg_real_error	1.21 Å
I(0) (real space) i0_real	1.5800e+08
I(0) uncertainty (real space) i0_real_error	3.1650e+06
Rg (reciprocal space) rg_reciprocal	36.57 Å
I(0) (reciprocal space) i0_reciprocal	158000000.0000
Solution quality estimate total_estimate	0.8739
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	37.2 Å
Skewness Skewness skewness	0.421
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	19400000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.848

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Hexon protein
Molecular weight formula_weight	107976.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	8005

ATPSMMPQWSYMHISGQDASEYLSPGLVQFARATETYFSLNNKFRNPTVAPTHDVTTDRSQRLTLRFIPVDREDTAYSYKARFTLAVGDNRVLDMASTYFDIRGVLDRGPTFKPYSGTAYNALAPKGAPNPCEWDEAATALEINLEEEDDDNEDEVDEQAEQQKTHVFGQAPYSGINITKEGIQIGVEGQTPKYADKTFQPEPQIGESQWYETEINHAAGRVLKKTTPMKPCYGSYAKPTNENGGQGILVKQQNGKLESQVEMQFFSTTEATAGNGDNLTPKVVLYSEDVDIETPDTHISYMPTIKEGNSRELMGQQSMPNRPNYIAFRDNFIGLMYYNSTGNMGVLAGQASQLNAVVDLQDRNTELSYQLLLDSIGDRTRYFSMWNQAVDSYDPDVRIIENHGTEDELPNYCFPLGGVINTETLTKVKPKTGQENGWEKDATEFSDKNEIRVGNNFAMEINLNANLWRNFLYSNIALYLPDKLKYSPSNVKISDNPNTYDYMNKRVVAPGLVDCYINLGARWSLDYMDNVNPFNHHRNAGLRYRSMLLGNGRYVPFHIQVPQKFFAIKNLLLLPGSYTYEWNFRKDVNMVLQSSLGNDLRVDGASIKFDSICLYATFFPMAHNTASTLEAMLRNDTNDQSFNDYLSAANMLYPIPANATNVPISIPSRNWAAFRGWAFTRLKTKETPSLGSGYDPYYTYSGSIPYLDGTFYLNHTFKKVAITFDSSVSWPGNDRLLTPNEFEIKRSVDGEGYNVAQCNMTKDWFLVQMLANYNIGYQGFYIPESYKDRMYSFFRNFQPMSRQVVDDTKYKDYQQVGILHQHNNSGFVGYLAPTMREGQAYPANFPYPLIGKTAVDSITQKKFLCDRTLWRIPFSSNFMSMGALTDLGQNLLYANSAHALDMTFEVDPMDEPTLLYVLFEVFDVVRVHRPHRGVIETVYLRTPFSAGNATT

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	800

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3tg7a1
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.2 — Group II dsDNA viruses VP
Family Family family	b.121.2.2 — Adenovirus hexon

Domain ID domain_id	d3tg7a2
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.2 — Group II dsDNA viruses VP
Family Family family	b.121.2.2 — Adenovirus hexon

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8. Citations (1)

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Unit-cell length a length_a	149.150 Å
Unit-cell length b length_b	149.150 Å
Unit-cell length c length_c	126.690 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	9

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	1.570 Å
Low-resolution limit resolution_low	45.550 Å
R factor r_factor	0.1858
R_work r_work	0.1838
R_free r_free	0.2227

fit	/app/data/saxs_computation/tg/3tg7/3tg7.fit
pddf	/app/data/pr_computation/tg/3tg7/3tg7.pr.out
profile	/app/data/saxs_computation/tg/3tg7/3tg7.dat

Crystal structure of Adenovirus serotype 5 hexon at 1.6A resolution

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

Hexon protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement