8i1v

The asymmetric unit of P22 procapsid

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

Major capsid protein

OrganismNot specified

UniProt P26747

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 14 Scaffolding protein × 7 (P26748) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CAPSD_BPP22
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–430; UniProt 1–430 Author chain B; PDBConstruct 1–430; UniProt 1–430 Author chain C; PDBConstruct 1–430; UniProt 1–430 Author chain D; PDBConstruct 1–430; UniProt 1–430 Author chain E; PDBConstruct 1–430; UniProt 1–430 Author chain F; PDBConstruct 1–430; UniProt 1–430 Author chain G; PDBConstruct 1–430; UniProt 1–430

Scaffolding protein

OrganismNot specified

UniProt P26748

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 14 Major capsid protein × 7 (P26747) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name VG08_BPP22
Isoform —
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–303; UniProt 1–303 Author chain I; PDBConstruct 1–303; UniProt 1–303 Author chain J; PDBConstruct 1–303; UniProt 1–303 Author chain K; PDBConstruct 1–303; UniProt 1–303 Author chain L; PDBConstruct 1–303; UniProt 1–303 Author chain M; PDBConstruct 1–303; UniProt 1–303 Author chain N; PDBConstruct 1–303; UniProt 1–303

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_id8i1v
Deposition date deposition_date2023-01-13
Structure title titleThe asymmetric unit of P22 procapsid
Keywords keywordsComplex, VIRUS, VIRAL PROTEIN; VIRAL PROTEIN
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.

8i1v__assembly_1__model_1

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

Download this curve (.dat)

8i1v__assembly_1__model_1 | I(q)

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

8i1v__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)52.46 Å
Rg (electron density)52.06 Å
Total Rg52.27 Å
Atom count23870
Residues3127
Excluded volume424170 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8i1v__assembly_1__model_1 tetradecameric (14) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8i1vB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily240 —
Domain ID domain_id8i1vC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily240 —
Domain ID domain_id8i1vD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily240 —
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7. Citations (1)