1fpn

HUMAN RHINOVIRUS SEROTYPE 2 (HRV2)

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

COAT PROTEIN VP1

OrganismNot specified

UniProt P04936

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 240 LAURIC ACID × 60 water × 240 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 LAURIC ACID × 1 water × 4 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 20 LAURIC ACID × 5 water × 20 Consistent with protein count
4 Protein homooligomer Homooligomer Protein 24 LAURIC ACID × 6 water × 24 Consistent with protein count
5 Protein homooligomer Homooligomer Protein 4 LAURIC ACID × 1 water × 4 Consistent with protein count
6 Protein homooligomer Homooligomer Protein 60 LAURIC ACID × 15 water × 60 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name POLG_HRV2
Isoform —
PDB entities 1, 2, 3, 4
Chains and sequence ranges Author chain 1; PDBConstruct 1–289; UniProt 568–856 Author chain 2; PDBConstruct 1–261; UniProt 70–330 Author chain 3; PDBConstruct 1–237; UniProt 331–567 Author chain 4; PDBConstruct 1–68; UniProt 2–69

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_id1fpn
Deposition date deposition_date2000-08-31
Structure title titleHUMAN RHINOVIRUS SEROTYPE 2 (HRV2)
Keywords keywordshuman rhinovirus, pocket factor, rhinovirus coat protein, 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.

1fpn__assembly_1__model_1

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

Download this curve (.dat)

1fpn__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.

1fpn__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)133.10 Å
Total Rg133.20 Å
Atom count369420
Residues46860
Excluded volume6549500 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1fpn__assembly_1__model_1 240-MERIC (240) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1fpn__assembly_2__model_1 tetrameric (4) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 1fpn__assembly_3__model_1 eicosameric (20) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 1fpn__assembly_4__model_1 24-meric (24) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 1fpn__assembly_5__model_1 tetrameric (4) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
6 1 1fpn__assembly_6__model_1 60-meric (60) 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 (6)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1fpn.1
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.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)
Domain ID domain_idd1fpn1_
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.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)
Domain ID domain_idd1fpn3_
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.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (3 domains)

Domain ID domain_id1fpn100
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1fpn200
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1fpn300
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20 —
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7. Citations (1)