1kvp

STRUCTURAL ANALYSIS OF THE SPIROPLASMA VIRUS, SPV4, IMPLICATIONS FOR EVOLUTIONARY VARIATION TO OBTAIN HOST DIVERSITY AMONG THE MICROVIRIDAE, ELECTRON MICROSCOPY, ALPHA CARBONS ONLY

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SPV4 CAPSID PROTEIN VP1

Enterobacteria phage phiX174

UniProt P03641

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 60 No other associated polymer Consistent with protein count
2 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count
3 Protein homooligomer Homooligomer Protein 5 No other associated polymer Consistent with protein count
4 Protein homooligomer Homooligomer Protein 6 No other associated polymer Consistent with protein count
5 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name VGF_BPPHX
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–497; UniProt 1–426

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_id1kvp
Deposition date deposition_date1997-12-12
Structure title titleSTRUCTURAL ANALYSIS OF THE SPIROPLASMA VIRUS, SPV4, IMPLICATIONS FOR EVOLUTIONARY VARIATION TO OBTAIN HOST DIVERSITY AMONG THE MICROVIRIDAE, ELECTRON MICROSCOPY, ALPHA CARBONS ONLY
Keywords keywordsBACTERIOPHAGE SPV4 COAT PROTEIN, CHIMERA, Icosahedral virus, Virus; VIRUS
Experimental Method methodELECTRON MICROSCOPY
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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.

1kvp__assembly_1__model_1

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

Download this curve (.dat)

1kvp__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.

1kvp__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)124.50 Å
Total Rg124.50 Å
Atom count0
Residues0
Excluded volume4081600 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1kvp__assembly_1__model_1 60-MERIC (60) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1kvp__assembly_2__model_1 monomeric (1) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 1kvp__assembly_3__model_1 pentameric (5) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 1kvp__assembly_4__model_1 hexameric (6) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 1kvp__assembly_5__model_1 monomeric (1) 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 (1)

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6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1kvpa_
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.5 — ssDNA viruses
Family Family familyb.121.5.1 — Microviridae-like VP
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7. Citations (3)