8yh0

A3R-Gi complex bound to NECA

Method: ELECTRON MICROSCOPY Dmax: 119.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

HA tag,Adenosine receptor A3,LgBiT,eGFP chimera

Ovis aries

UniProt A0A5P9VSM6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 2–239 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1 × 2 (P59768,P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5P9VSM6_HRSV
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 544–781; UniProt 2–239

HA tag,Adenosine receptor A3,LgBiT,eGFP chimera

Ovis aries

UniProt P03435

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 1–16 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1 × 2 (P59768,P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I75A3
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–16; UniProt 1–16

HA tag,Adenosine receptor A3,LgBiT,eGFP chimera

Ovis aries

UniProt W5QED6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 2–317 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1 × 2 (P59768,P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W5QED6_SHEEP
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 27–342; UniProt 2–317

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1

Homo sapiens

UniProt P59768

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–71 Chain G; UniProt 1–71 Not recorded HA tag,Adenosine receptor A3,LgBiT,eGFP chimera × 1 (P03435,W5QED6,A0A5P9VSM6) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

1233 other PDB entries and 1236 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–71; UniProt 1–71 Author chain G; PDBConstruct 1–71; UniProt 1–71

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1

Homo sapiens

UniProt P63096

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 3–354 Chain G; UniProt 3–354 Not recorded HA tag,Adenosine receptor A3,LgBiT,eGFP chimera × 1 (P03435,W5QED6,A0A5P9VSM6) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

573 other PDB entries and 591 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 82–433; UniProt 3–354 Author chain G; PDBConstruct 82–433; UniProt 3–354

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

Rattus rattus

UniProt P62871

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded HA tag,Adenosine receptor A3,LgBiT,eGFP chimera × 1 (P03435,W5QED6,A0A5P9VSM6) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,Guanine nucleotide-binding protein G(i) subunit alpha-1 × 2 (P59768,P63096) scfv16 × 1 NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

72 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 7–345; UniProt 2–340

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8yh0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yh0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yh0
Deposition date deposition_date2024-02-27
Structure title titleA3R-Gi complex bound to NECA
Keywords keywordsGPCR, complex, adenosine receptor, adenosine, g protein, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.05
Radius of gyration Rg (electron density) rg_electron36.86
Forward intensity I(0) i0225782000.00
Molecular weight molecular_weight123810.0 kDa
Excluded volume excluded_volume155900 ų
Envelope volume envelope_volume201830 ų
Hydration-shell volume shell_volume46645 ų
Envelope diameter envelope_diameter126.9
Shell Rg shell_rg41.65
Envelope Rg envelope_rg36.88
Shape Rg shape_rg36.83
Total Rg total_rg37.27
Total atoms total_atoms8693
Residues n_residues1103
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax119.5
Rg (real space) rg_real36.99
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real2.2580e+08
I(0) uncertainty (real space) i0_real_error3.7810e+06
Rg (reciprocal space) rg_reciprocal37.03
I(0) (reciprocal space) i0_reciprocal225800000.0000
Solution quality estimate total_estimate0.8987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.600
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39330000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)