1em9

ROUS SARCOMA VIRUS CAPSID PROTEIN: N-TERMINAL DOMAIN

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

GAG POLYPROTEIN CAPSID PROTEIN P27

Rous sarcoma virus - Prague C

UniProt P03322

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 MAGNESIUM ION × 1 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GAG_RSVP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–154; UniProt 240–393 Author chain B; PDBConstruct 1–154; UniProt 240–393

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_id1em9
Deposition date deposition_date2000-03-16
Structure title titleROUS SARCOMA VIRUS CAPSID PROTEIN: N-TERMINAL DOMAIN
Keywords keywordsVIRUS/VIRAL PROTEIN, Viral protein; VIRAL PROTEIN
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.

1em9__assembly_1__model_1

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

Download this curve (.dat)

1em9__assembly_1__model_1 | I(q)

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

1em9__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)16.75 Å
Rg (electron density)15.52 Å
Total Rg16.63 Å
Atom count1108
Residues147
Excluded volume19889 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1em9__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1em9__assembly_2__model_1 monomeric (1) 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 (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1em9a_
Class classa — All alpha proteins
Fold Fold folda.73 — Retrovirus capsid protein, N-terminal core domain
Superfamily Superfamily superfamilya.73.1 — Retrovirus capsid protein, N-terminal core domain
Family Family familya.73.1.1 — Retrovirus capsid protein, N-terminal core domain
Domain ID domain_idd1em9b_
Class classa — All alpha proteins
Fold Fold folda.73 — Retrovirus capsid protein, N-terminal core domain
Superfamily Superfamily superfamilya.73.1 — Retrovirus capsid protein, N-terminal core domain
Family Family familya.73.1.1 — Retrovirus capsid protein, N-terminal core domain

CATH v4.4 (2 domains)

Domain ID domain_id1em9A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology375 — Human Immunodeficiency Virus Type 1 Capsid Protein
Homologous superfamily homologous superfamily10 — Human Immunodeficiency Virus Type 1 Capsid Protein
Domain ID domain_id1em9B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology375 — Human Immunodeficiency Virus Type 1 Capsid Protein
Homologous superfamily homologous superfamily10 — Human Immunodeficiency Virus Type 1 Capsid Protein
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7. Citations (1)