SAXSdb — 1cov

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

COXSACKIEVIRUS COAT 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 × 240 PDB declaration: 240-MERIC（240） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å
3	Protein homooligomer Homooligomer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å
4	Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å
5	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å
6	Protein homooligomer Homooligomer Protein × 480 PDB declaration: 480-meric（480） Consistent with protein copy count	Chain 1； UniProt 571–851 Chain 2； UniProt 70–332 Chain 3； UniProt 333–570 Chain 4； UniProt 2–69	Not recorded	PLM PALMITIC ACID × 120 MYR MYRISTIC ACID × 120	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 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 1COV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1JEW CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR). Deposited 2001-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain 1 571–851（281 aa） Fragment：Residues 571-851 Chain 2 70–332（263 aa） Fragment：Residues 70-332 Chain 3 333–570（238 aa） Fragment：Residues 333-570 Chain 4 2–69（68 aa） Fragment：Residues 2-69	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER. X-ray crystallization conditions ELECTRON MICROSCOPY RECONSTRUCTION；pH 7.5；298 K；WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K	Resolution 22.00 Å
1JEW CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR). Deposited 2001-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 571–851（281 aa） Fragment：Residues 571-851 Chain 2 70–332（263 aa） Fragment：Residues 70-332 Chain 3 333–570（238 aa） Fragment：Residues 333-570 Chain 4 2–69（68 aa） Fragment：Residues 2-69	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER. X-ray crystallization conditions ELECTRON MICROSCOPY RECONSTRUCTION；pH 7.5；298 K；WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K	Resolution 22.00 Å
1JEW CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR). Deposited 2001-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain 1 571–851（281 aa） Fragment：Residues 571-851 Chain 2 70–332（263 aa） Fragment：Residues 70-332 Chain 3 333–570（238 aa） Fragment：Residues 333-570 Chain 4 2–69（68 aa） Fragment：Residues 2-69	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER. X-ray crystallization conditions ELECTRON MICROSCOPY RECONSTRUCTION；pH 7.5；298 K；WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K	Resolution 22.00 Å
1JEW CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR). Deposited 2001-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 1 571–851（281 aa） Fragment：Residues 571-851 Chain 2 70–332（263 aa） Fragment：Residues 70-332 Chain 3 333–570（238 aa） Fragment：Residues 333-570 Chain 4 2–69（68 aa） Fragment：Residues 2-69	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER. X-ray crystallization conditions ELECTRON MICROSCOPY RECONSTRUCTION；pH 7.5；298 K；WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K	Resolution 22.00 Å
1JEW CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR). Deposited 2001-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 571–851（281 aa） Fragment：Residues 571-851 Chain 2 70–332（263 aa） Fragment：Residues 70-332 Chain 3 333–570（238 aa） Fragment：Residues 333-570 Chain 4 2–69（68 aa） Fragment：Residues 2-69	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER. X-ray crystallization conditions ELECTRON MICROSCOPY RECONSTRUCTION；pH 7.5；298 K；WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K	Resolution 22.00 Å
3JD7 The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs Deposited 2016-04-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-meric	Chain 1 571–851（281 aa） Fragment：UNP residues 571-851 Chain 2 70–332（263 aa） Fragment：UNP residues 70-332 Chain 3 333–570（238 aa） Fragment：UNP residues 333-570 Chain 4 2–69（68 aa） Fragment：UNP residues 2-69	Not recorded	PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM vitrification conditions 102 K；Cryogen ETHANE；Plunged into liquid ethane (GATAN CRYOPLUNGE 3)	Resolution 3.90 Å
3JD7 The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs Deposited 2016-04-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 571–851（281 aa） Fragment：UNP residues 571-851 Chain 2 70–332（263 aa） Fragment：UNP residues 70-332 Chain 3 333–570（238 aa） Fragment：UNP residues 333-570 Chain 4 2–69（68 aa） Fragment：UNP residues 2-69	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM vitrification conditions 102 K；Cryogen ETHANE；Plunged into liquid ethane (GATAN CRYOPLUNGE 3)	Resolution 3.90 Å
3JD7 The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs Deposited 2016-04-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain 1 571–851（281 aa） Fragment：UNP residues 571-851 Chain 2 70–332（263 aa） Fragment：UNP residues 70-332 Chain 3 333–570（238 aa） Fragment：UNP residues 333-570 Chain 4 2–69（68 aa） Fragment：UNP residues 2-69	Not recorded	PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM vitrification conditions 102 K；Cryogen ETHANE；Plunged into liquid ethane (GATAN CRYOPLUNGE 3)	Resolution 3.90 Å
3JD7 The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs Deposited 2016-04-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain 1 571–851（281 aa） Fragment：UNP residues 571-851 Chain 2 70–332（263 aa） Fragment：UNP residues 70-332 Chain 3 333–570（238 aa） Fragment：UNP residues 333-570 Chain 4 2–69（68 aa） Fragment：UNP residues 2-69	Not recorded	PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM vitrification conditions 102 K；Cryogen ETHANE；Plunged into liquid ethane (GATAN CRYOPLUNGE 3)	Resolution 3.90 Å
3JD7 The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs Deposited 2016-04-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 571–851（281 aa） Fragment：UNP residues 571-851 Chain 2 70–332（263 aa） Fragment：UNP residues 70-332 Chain 3 333–570（238 aa） Fragment：UNP residues 333-570 Chain 4 2–69（68 aa） Fragment：UNP residues 2-69	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM vitrification conditions 102 K；Cryogen ETHANE；Plunged into liquid ethane (GATAN CRYOPLUNGE 3)	Resolution 3.90 Å

2 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_CXB3W
Isoform	—
PDB entities	1, 2, 3, 4
Chains and sequence ranges	Author chain 1； PDBConstruct 1–281； UniProt 571–851 Author chain 2； PDBConstruct 1–263； UniProt 70–332 Author chain 3； PDBConstruct 1–238； UniProt 333–570 Author chain 4； PDBConstruct 1–68； UniProt 2–69

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	1cov
Deposition date deposition_date	1994-10-19
Structure title title	COXSACKIEVIRUS B3 COAT PROTEIN
Keywords keywords	COXSACKIEVIRUS B3, Icosahedral virus, Virus; VIRUS
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	29.54 Å
Radius of gyration Rg (electron density) rg_electron	28.51 Å
Forward intensity I(0) i0	133909000.00
Molecular weight molecular_weight	91130.0 kDa
Excluded volume excluded_volume	113680 Å³
Envelope volume envelope_volume	138500 Å³
Hydration-shell volume shell_volume	39607 Å³
Envelope diameter envelope_diameter	105.1 Å
Shell Rg shell_rg	36.51 Å
Envelope Rg envelope_rg	29.24 Å
Shape Rg shape_rg	28.50 Å
Total Rg total_rg	29.28 Å
Total atoms total_atoms	6409
Residues n_residues	818
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	98.1 Å
Rg (real space) rg_real	29.51 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	1.3390e+08
I(0) uncertainty (real space) i0_real_error	1.8170e+06
Rg (reciprocal space) rg_reciprocal	29.53 Å
I(0) (reciprocal space) i0_reciprocal	133900000.0000
Solution quality estimate total_estimate	0.8835
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.5 Å
Skewness Skewness skewness	0.361
Kurtosis Kurtosis kurtosis	-0.217
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23410000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.838; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.968

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	COXSACKIEVIRUS COAT PROTEIN
Molecular weight formula_weight	31380.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	6409

GPVEDAITAAIGRVADTVGTGPTNSEAIPALTAAETGHTSQVVPSDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVITPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSVPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNT

Entity 2 Entity 2 polymer

Description description	COXSACKIEVIRUS COAT PROTEIN
Molecular weight formula_weight	28877.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SPTVEECGYSDRVRSITLGNSTITTQECANVVVGYGVWPDYLKDSEATAEDQPTQPDVATCRFYTLDSVQWQKTSPGWWWKLPDALSNLGLFGQNMQYHYLGRTGYTIHVQCNASKFHQGCLLVVCVPEAEMGCATLNNTPSSAELLGGDTAKEFADKPVASGSNKLVQRVVYNAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYTNSVPMDNMFRHNNVTLMVIPFVPLDYCPGSTTYVPITVTIAPMCAEYNGLRLAGHQ

Entity 3 Entity 3 polymer

Description description	COXSACKIEVIRUS COAT PROTEIN
Molecular weight formula_weight	26198.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPTMNTPGSCQFLTSDDFQSPSAMPQYDVTPEMRIPGEVKNLMEIAEVDSVVPVQNVGEKVNSMEAYQIPVRSNEGSGTQVFGFPLQPGYSSVFSRTLLGEILNYYTHWSGSIKLTFMFCGSAMATGKFLLAYSPPGAGAPTKRVDAMLGTHVVWDVGLQSSCVLCIPWISQTHYRYVASDEYTAGGFITCWYQTNIVVPADAQSSCYIMCFVSACNDFSVRLLKDTPFISQENFFQ

Entity 4 Entity 4 polymer

Description description	COXSACKIEVIRUS COAT PROTEIN
Molecular weight formula_weight	7379.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSTQKTGAHETGLNASGNSIIHYTNINYYKDAASNSANRQDFTQDPSKFTEPVKDIMIKSLPALN

Entity 5 Entity 5 non-polymer

Description description	PALMITIC ACID
Molecular weight formula_weight	256.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1cov.1
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1cov1_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1cov3_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (4 domains)

Domain ID domain_id	1cov100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1cov200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1cov300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1cov400
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	80 — Rhinovirus 14, subunit 4
Homologous superfamily homologous superfamily	10 — Picornavirus coat protein VP4

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8. Citations (2)

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Unit-cell length a length_a	574.620 Å
Unit-cell length b length_b	302.070 Å
Unit-cell length c length_c	521.610 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.70 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	240

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2640
R_work r_work	0.2640
R_free r_free	—

fit	/app/data/saxs_computation/co/1cov/1cov.fit
pddf	/app/data/pr_computation/co/1cov/1cov.pr.out
profile	/app/data/saxs_computation/co/1cov/1cov.dat

COXSACKIEVIRUS B3 COAT PROTEIN

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

COXSACKIEVIRUS COAT 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

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)