3raa

Structural studies of AAV8 capsid transitions associated with endosomal trafficking

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

Capsid protein

Adeno-associated virus - 8

UniProt Q8JQF8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 60 ADENOSINE MONOPHOSPHATE × 60 Consistent with protein count
2 Protein monomer Monomer Protein 1 ADENOSINE MONOPHOSPHATE × 1 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 5 ADENOSINE MONOPHOSPHATE × 5 Consistent with protein count
4 Protein homooligomer Homooligomer Protein 6 ADENOSINE MONOPHOSPHATE × 6 Consistent with protein count
5 Protein monomer Monomer Protein 1 ADENOSINE MONOPHOSPHATE × 1 Consistent with protein count
6 Protein homooligomer Homooligomer Protein 10 ADENOSINE MONOPHOSPHATE × 10 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q8JQF8_9VIRU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–519; UniProt 220–738

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_id3raa
Deposition date deposition_date2011-03-27
Structure title titleStructural studies of AAV8 capsid transitions associated with endosomal trafficking
Keywords keywordsBeta Barrel, Viral Capsid, 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.

3raa__assembly_1__model_1

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

Download this curve (.dat)

3raa__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 109 1010 1011 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3raa__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)109.40 Å
Total Rg109.60 Å
Atom count249240
Residues31140
Excluded volume4356100 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3raa__assembly_1__model_1 60-MERIC (60) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3raa__assembly_2__model_1 monomeric (1) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 3raa__assembly_3__model_1 pentameric (5) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 3raa__assembly_4__model_1 hexameric (6) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 3raa__assembly_5__model_1 monomeric (1) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
6 1 3raa__assembly_6__model_1 decameric (10) 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 (2)

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3raaA00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology30 — Empty Capsid Viral Protein 2
Homologous superfamily homologous superfamily10 — Parvovirus coat protein VP1/VP2
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7. Citations (1)