9uy3

Anamorelin bound growth hormone secretagogue receptor in complex with Gq

Method: ELECTRON MICROSCOPY Dmax: 121.5 Å Quality: GOOD

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

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

Homo sapiens

UniProt P62873

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 Engineered G-alpha-q subunit × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) NB35 × 1 ;Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,human growth hormone secretagogue receptor ; × 1 (P0ABE7,Q92847) CLR CHOLESTEROL × 2 A1ESD 2-azanyl-N-[(2R)-1-[(3S)-3-[dimethylamino(methyl)carbamoyl]-3-(phenylmethyl)piperidin-1-yl]-3-(1H-indol-3-yl)-1-oxidanylidene-propan-2-yl]-2-methyl-propanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–345; 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 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 G; UniProt 1–71 Not recorded Engineered G-alpha-q subunit × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) NB35 × 1 ;Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,human growth hormone secretagogue receptor ; × 1 (P0ABE7,Q92847) CLR CHOLESTEROL × 2 A1ESD 2-azanyl-N-[(2R)-1-[(3S)-3-[dimethylamino(methyl)carbamoyl]-3-(phenylmethyl)piperidin-1-yl]-3-(1H-indol-3-yl)-1-oxidanylidene-propan-2-yl]-2-methyl-propanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

;Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,human growth hormone secretagogue receptor ;

Homo sapiens

UniProt P0ABE7

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 23–128 Not recorded Engineered G-alpha-q subunit × 1 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) NB35 × 1 CLR CHOLESTEROL × 2 A1ESD 2-azanyl-N-[(2R)-1-[(3S)-3-[dimethylamino(methyl)carbamoyl]-3-(phenylmethyl)piperidin-1-yl]-3-(1H-indol-3-yl)-1-oxidanylidene-propan-2-yl]-2-methyl-propanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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.

714 other PDB entries and 822 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C562_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 42–147; UniProt 23–128

;Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,Soluble cytochrome b562,Growth hormone secretagogue receptor type 1,human growth hormone secretagogue receptor ;

Homo sapiens

UniProt Q92847

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 1–366 Not recorded Engineered G-alpha-q subunit × 1 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) NB35 × 1 CLR CHOLESTEROL × 2 A1ESD 2-azanyl-N-[(2R)-1-[(3S)-3-[dimethylamino(methyl)carbamoyl]-3-(phenylmethyl)piperidin-1-yl]-3-(1H-indol-3-yl)-1-oxidanylidene-propan-2-yl]-2-methyl-propanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GHSR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 148–513; UniProt 1–366

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 9uy3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9uy3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9uy3
Deposition date deposition_date2025-05-14
Structure title titleAnamorelin bound growth hormone secretagogue receptor in complex with Gq
Keywords keywordsgrowth hormone secretagogue receptor, GHSR, Anamorelin, ghrelin receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.24
Radius of gyration Rg (electron density) rg_electron35.31
Forward intensity I(0) i0405345000.00
Molecular weight molecular_weight108950.0 kDa
Excluded volume excluded_volume105490 ų
Envelope volume envelope_volume184560 ų
Hydration-shell volume shell_volume44735 ų
Envelope diameter envelope_diameter128.7
Shell Rg shell_rg40.47
Envelope Rg envelope_rg35.38
Shape Rg shape_rg35.33
Total Rg total_rg35.53
Total atoms total_atoms8245
Residues n_residues1034
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 dmax121.5
Rg (real space) rg_real35.41
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real4.0530e+08
I(0) uncertainty (real space) i0_real_error7.5340e+06
Rg (reciprocal space) rg_reciprocal35.31
I(0) (reciprocal space) i0_reciprocal405300000.0000
Solution quality estimate total_estimate0.8578
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47670000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.812

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)