2ebo

CORE STRUCTURE OF GP2 FROM EBOLA VIRUS

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

EBOLA VIRUS ENVELOPE GLYCOPROTEIN

Zaire ebolavirus - Mayinga (Zaire, 1976)

UniProt Q05320

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 3 CHLORIDE ION × 1 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name VGP_EBOZM
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 557–630 Author chain B; PDBConstruct 1–74; UniProt 557–630 Author chain C; PDBConstruct 1–74; UniProt 557–630

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_id2ebo
Deposition date deposition_date1998-12-24
Structure title titleCORE STRUCTURE OF GP2 FROM EBOLA VIRUS
Keywords keywordsENVELOPE GLYCOPROTEIN, FILOVIRUS, EBOLA VIRUS, GP2, COAT PROTEIN; ENVELOPE GLYCOPROTEIN
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.

2ebo__assembly_1__model_1

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

Download this curve (.dat)

2ebo__assembly_1__model_1 | I(q)

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

2ebo__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)20.64 Å
Rg (electron density)19.90 Å
Total Rg20.62 Å
Atom count1807
Residues222
Excluded volume32149 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2ebo__assembly_1__model_1 trimeric (3) 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) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2eboa_
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.2 — Virus ectodomain
Family Family familyh.3.2.1 — Virus ectodomain
Domain ID domain_idd2ebob_
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.2 — Virus ectodomain
Family Family familyh.3.2.1 — Virus ectodomain
Domain ID domain_idd2eboc_
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.2 — Virus ectodomain
Family Family familyh.3.2.1 — Virus ectodomain

CATH v4.4 (3 domains)

Domain ID domain_id2eboA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily210 —
Domain ID domain_id2eboB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily210 —
Domain ID domain_id2eboC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily210 —
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7. Citations (3)