1opo

THE STRUCTURE OF CARNATION MOTTLE VIRUS

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Coat protein

OrganismNot specified

UniProt P04383

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 180 SULFATE ION × 180 CALCIUM ION × 60 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 3 SULFATE ION × 3 CALCIUM ION × 1 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 15 SULFATE ION × 15 CALCIUM ION × 5 Consistent with protein count
4 Protein homooligomer Homooligomer Protein 18 SULFATE ION × 18 CALCIUM ION × 6 Consistent with protein count
5 Protein homooligomer Homooligomer Protein 3 SULFATE ION × 3 CALCIUM ION × 1 Consistent with protein count
6 Protein homooligomer Homooligomer Protein 15 SULFATE ION × 15 CALCIUM ION × 5 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name COAT_CARMV
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–348; UniProt 1–348 Author chain B; PDBConstruct 1–348; UniProt 1–348 Author chain C; PDBConstruct 1–348; UniProt 1–348

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_id1opo
Deposition date deposition_date2003-03-06
Structure title titleTHE STRUCTURE OF CARNATION MOTTLE VIRUS
Keywords keywordsPLANT VIRUS, CARMOVIRUS, VIRUS/VIRAL PROTEIN, TOMATO BUSHY STUNT VIRUS, Icosahedral virus, Virus; VIRUS
Experimental Method methodX-RAY DIFFRACTION
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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.

1opo__assembly_1__model_1

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

Download this curve (.dat)

1opo__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 1011 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1opo__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)144.00 Å
Total Rg144.00 Å
Atom count367800
Residues48120
Excluded volume6594700 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1opo__assembly_1__model_1 complete icosahedral assembly (180) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1opo__assembly_2__model_1 trimeric (3) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 1opo__assembly_3__model_1 pentadecameric (15) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 1opo__assembly_4__model_1 octadecameric (18) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 1opo__assembly_5__model_1 trimeric (3) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
6 1 1opo__assembly_6__model_1 pentadecameric (15) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1opoa_
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.121.4.7 — Tombusviridae-like VP
Domain ID domain_idd1opob_
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.121.4.7 — Tombusviridae-like VP
Domain ID domain_idd1opoc_
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.121.4.7 — Tombusviridae-like VP

CATH v4.4 (6 domains)

Domain ID domain_id1opoA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1opoA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1780 — Carmovirus coat protein
Domain ID domain_id1opoB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1opoB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1780 — Carmovirus coat protein
Domain ID domain_id1opoC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1opoC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1780 — Carmovirus coat protein
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7. Citations (1)