8x79

MRE-269 bound Prostacyclin Receptor G protein complex

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

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,GNAS complex locus,GNAS complex locus

Homo sapiens

UniProt A0A590UJY2

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Nanobody35 × 1 Prostacyclin receptor × 1 (P43119) 2-[4-[(5,6-diphenylpyrazin-2-yl)-propan-2-yl-amino]butoxy]ethanoic acid × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A590UJY2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 69–249; UniProt 47–237

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,GNAS complex locus,GNAS complex locus × 1 (A0A590UJY2) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Nanobody35 × 1 Prostacyclin receptor × 1 (P43119) 2-[4-[(5,6-diphenylpyrazin-2-yl)-propan-2-yl-amino]butoxy]ethanoic acid × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 12–350; UniProt 2–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Homo sapiens

UniProt P59768

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,GNAS complex locus,GNAS complex locus × 1 (A0A590UJY2) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Nanobody35 × 1 Prostacyclin receptor × 1 (P43119) 2-[4-[(5,6-diphenylpyrazin-2-yl)-propan-2-yl-amino]butoxy]ethanoic acid × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

Prostacyclin receptor

Homo sapiens

UniProt P43119

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,GNAS complex locus,GNAS complex locus × 1 (A0A590UJY2) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Nanobody35 × 1 2-[4-[(5,6-diphenylpyrazin-2-yl)-propan-2-yl-amino]butoxy]ethanoic acid × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PI2R_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 1–386; UniProt 1–386

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_id8x79
Deposition date deposition_date2023-11-23
Last revision last_revision2024-03-06
Structure title titleMRE-269 bound Prostacyclin Receptor G protein complex
Keywords keywordsAgonist, Complex, lipid receptor, SIGNALING PROTEIN; SIGNALING 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.

8x79__assembly_1__model_1

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

Download this curve (.dat)

8x79__assembly_1__model_1 | I(q)

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

8x79__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)34.93 Å
Rg (electron density)34.71 Å
Total Rg35.19 Å
Atom count16176
Residues1055
Excluded volume144880 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8x79__assembly_1__model_1 pentameric (5) 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 (6)

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7. Citations (1)