← Back to search
1qbe

BACTERIOPHAGE Q BETA CAPSID

Method: X-RAY DIFFRACTION
▼

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

BACTERIOPHAGE Q BETA CAPSID

OrganismNot specified

UniProt P03615

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 180 No other associated polymer Consistent with protein count
2 Protein homooligomer Homooligomer Protein 3 No other associated polymer Consistent with protein count
3 Protein homooligomer Homooligomer Protein 15 No other associated polymer Consistent with protein count
4 Protein homooligomer Homooligomer Protein 18 No other associated polymer Consistent with protein count
5 Protein homooligomer Homooligomer Protein 3 No other associated polymer Consistent with protein count
6 Protein homooligomer Homooligomer Protein 90 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer
7lge 7lge

2 assemblies

Other homooligomers
1qbe 1qbe 1qbe 1qbe 1qbe 1qbe 5kip 5kip 5kip 5kip 5kip 5vly

28 assemblies; showing the first 12

Heteromeric or nucleic-acid complex
4l8h 5vlz 7lhd

3 assemblies

View Construct and Data Evidence
UniProt name COAT_BPQBE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–132； UniProt 1–132 Author chain B； PDBConstruct 1–132； UniProt 1–132 Author chain C； PDBConstruct 1–132； UniProt 1–132

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1qbe
Deposition date deposition_date1996-01-10
Structure title titleBACTERIOPHAGE Q BETA CAPSID
Keywords keywordsCOAT PROTEIN, RNA BINDING, Icosahedral virus, Virus; VIRUS
Experimental Method methodX-RAY DIFFRACTION
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1qbe__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1qbe__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1qbe__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）0.00 Å
Rg (electron density)127.30 Å
Total Rg127.40 Å
Atom count168480
Residues22680
Excluded volume2995400 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1qbe__assembly_1__model_1 complete icosahedral assembly （180） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1qbe__assembly_2__model_1 trimeric （3） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 1qbe__assembly_3__model_1 pentadecameric （15） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 1qbe__assembly_4__model_1 octadecameric （18） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 1qbe__assembly_5__model_1 trimeric （3） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6 1 1qbe__assembly_6__model_1 90-meric （90） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1qbea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.85 — RNA bacteriophage capsid protein
Superfamily Superfamily superfamilyd.85.1 — RNA bacteriophage capsid protein
Family Family familyd.85.1.1 — RNA bacteriophage capsid protein
Domain ID domain_idd1qbeb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.85 — RNA bacteriophage capsid protein
Superfamily Superfamily superfamilyd.85.1 — RNA bacteriophage capsid protein
Family Family familyd.85.1.1 — RNA bacteriophage capsid protein
Domain ID domain_idd1qbec_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.85 — RNA bacteriophage capsid protein
Superfamily Superfamily superfamilyd.85.1 — RNA bacteriophage capsid protein
Family Family familyd.85.1.1 — RNA bacteriophage capsid protein

CATH v4.4 (3 domains)

Domain ID domain_id1qbeA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology380 — MS2 Viral Coat Protein
Homologous superfamily homologous superfamily10 — MS2 Viral Coat Protein
Domain ID domain_id1qbeB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology380 — MS2 Viral Coat Protein
Homologous superfamily homologous superfamily10 — MS2 Viral Coat Protein
Domain ID domain_id1qbeC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology380 — MS2 Viral Coat Protein
Homologous superfamily homologous superfamily10 — MS2 Viral Coat Protein
▶

7. Citations (2)