← Back to search
1bev

BOVINE ENTEROVIRUS VG-5-27

Method: X-RAY DIFFRACTION Dmax: 94.6 Å Quality: GOOD
▼

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

BOVINE ENTEROVIRUS COAT PROTEINS VP1 TO VP4

Bovine enterovirus (STRAIN VG-5-27)

UniProt P12915

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 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 120 MYR MYRISTIC ACID × 60 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain 1； UniProt 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 2 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å
3 Protein homooligomer Homooligomer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count Chain 1； UniProt 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 10 MYR MYRISTIC ACID × 5 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å
4 Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count Chain 1； UniProt 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 12 MYR MYRISTIC ACID × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å
5 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain 1； UniProt 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 2 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å
6 Protein homooligomer Homooligomer Protein × 240 PDB declaration: 240-meric（240） Consistent with protein copy count Chain 1； UniProt 559–839 Chain 2； UniProt 69–316 Chain 3； UniProt 317–558 Chain 4； UniProt 1–68 Not recorded SO4 SULFATE ION × 120 MYR MYRISTIC ACID × 60 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 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 1BEV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6THD Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E Deposited 2019-11-19 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 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 120 SO4 SULFATE ION × 120 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.23 Å
6THD Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E Deposited 2019-11-19 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 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 2 SO4 SULFATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.23 Å
6THD Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E Deposited 2019-11-19 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 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 10 SO4 SULFATE ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.23 Å
6THD Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E Deposited 2019-11-19 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 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 12 SO4 SULFATE ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.23 Å
6THD Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E Deposited 2019-11-19 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 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 2 SO4 SULFATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.23 Å
6THN Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification Deposited 2019-11-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Homooligomer；Protein × 240 PDB declaration: 300-meric
Chain 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 120 SO4 SULFATE ION × 120 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6THN Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification Deposited 2019-11-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–RNA Homooligomer；Protein × 4 PDB declaration: pentameric
Chain 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 2 SO4 SULFATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6THN Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification Deposited 2019-11-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–RNA Homooligomer；Protein × 20 PDB declaration: 25-meric
Chain 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 10 SO4 SULFATE ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6THN Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification Deposited 2019-11-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–RNA Homooligomer；Protein × 24 PDB declaration: 30-meric
Chain 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 12 SO4 SULFATE ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6THN Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification Deposited 2019-11-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein–RNA Homooligomer；Protein × 4 PDB declaration: pentameric
Chain 1 560–840（281 aa）
Chain 2 70–317（248 aa）
Chain 3 318–559（242 aa）
Chain 4 18–69（52 aa）
Not recorded MYR MYRISTIC ACID × 2 SO4 SULFATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å

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

View Construct and Data Evidence
UniProt name POLG_BOVEV
Isoform —
PDB entities 1, 2, 3, 4
Chains and sequence ranges Author chain 1； PDBConstruct 1–281； UniProt 559–839 Author chain 2； PDBConstruct 1–248； UniProt 69–316 Author chain 3； PDBConstruct 1–242； UniProt 317–558 Author chain 4； PDBConstruct 1–68； UniProt 1–68

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 1bev

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bev
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bev
Deposition date deposition_date1996-04-03
Structure title titleBOVINE ENTEROVIRUS VG-5-27
Keywords keywordsCOAT PROTEIN, BOVINE ENTEROVIRUS VG-5-27, PICORNAVIRUS, Icosahedral virus, Virus; VIRUS
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier29.10 Å
Radius of gyration Rg (electron density) rg_electron28.04 Å
Forward intensity I(0) i0125729000.00
Molecular weight molecular_weight87770.0 kDa
Excluded volume excluded_volume109310 ų
Envelope volume envelope_volume134290 ų
Hydration-shell volume shell_volume39011 ų
Envelope diameter envelope_diameter101.3 Å
Shell Rg shell_rg36.20 Å
Envelope Rg envelope_rg28.55 Å
Shape Rg shape_rg28.02 Å
Total Rg total_rg28.86 Å
Total atoms total_atoms6185
Residues n_residues794
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
▼

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

Maximum dimension Dmax dmax94.6 Å
Rg (real space) rg_real29.04 Å
Rg uncertainty (real space) rg_real_error0.47 Å
I(0) (real space) i0_real1.2570e+08
I(0) uncertainty (real space) i0_real_error1.7190e+06
Rg (reciprocal space) rg_reciprocal29.07 Å
I(0) (reciprocal space) i0_reciprocal125700000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.0 Å
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22340000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.977
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (7)

▼

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1bev.1
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)
Domain ID domain_idd1bev1_
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)
Domain ID domain_idd1bev3_
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (4 domains)

Domain ID domain_id1bev100
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1bev200
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1bev300
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1bev400
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology80 — Rhinovirus 14, subunit 4
Homologous superfamily homologous superfamily10 — Picornavirus coat protein VP4
▶

8. Citations (4)

▶

9. Files and Curves (10)