8wa3

Cryo-EM structure of peptide free and Gs-coupled GIPR

Method: ELECTRON MICROSCOPY Dmax: 111.8 Å Quality: GOOD

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

Gastric inhibitory polypeptide receptor,Fusion protein

Homo sapiens

UniProt P48546

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 22–421 Mutation:T345F Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (P04896) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1,O-antigen polymerase × 1 (P54311,A0A0P6XLS5) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody-35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GIPR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–400; UniProt 22–421

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Bos taurus

UniProt P04896

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 1–394 Mutation:S54N, G226A, E268A, N271K, K274D, R280K, T284D, I285T, A366S Gastric inhibitory polypeptide receptor,Fusion protein × 1 (P48546) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1,O-antigen polymerase × 1 (P54311,A0A0P6XLS5) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody-35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAS2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–394; UniProt 1–394

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1,O-antigen polymerase

Leptolinea tardivitalis

UniProt A0A0P6XLS5

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 218–225 Not recorded Gastric inhibitory polypeptide receptor,Fusion protein × 1 (P48546) Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (P04896) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody-35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0P6XLS5_9CHLR
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 364–371; UniProt 218–225

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1,O-antigen polymerase

Leptolinea tardivitalis

UniProt P54311

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 Gastric inhibitory polypeptide receptor,Fusion protein × 1 (P48546) Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (P04896) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody-35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

161 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_RAT
Isoform
PDB entities 3
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

Bos taurus

UniProt P63212

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 Gastric inhibitory polypeptide receptor,Fusion protein × 1 (P48546) Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (P04896) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1,O-antigen polymerase × 1 (P54311,A0A0P6XLS5) Nanobody-35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

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 8wa3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wa3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wa3
Deposition date deposition_date2023-09-06
Structure title titleCryo-EM structure of peptide free and Gs-coupled GIPR
Keywords keywords;Glucose-dependent insulinotropic polypeptide receptor; cryo-electron microscopy; G protein-coupled receptor; ligand recognition, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.22
Radius of gyration Rg (electron density) rg_electron34.14
Forward intensity I(0) i0212687000.00
Molecular weight molecular_weight116100.0 kDa
Excluded volume excluded_volume145060 ų
Envelope volume envelope_volume189810 ų
Hydration-shell volume shell_volume46757 ų
Envelope diameter envelope_diameter119.9
Shell Rg shell_rg40.12
Envelope Rg envelope_rg34.37
Shape Rg shape_rg34.13
Total Rg total_rg34.63
Total atoms total_atoms8163
Residues n_residues1031
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 dmax111.8
Rg (real space) rg_real34.28
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.1270e+08
I(0) uncertainty (real space) i0_real_error3.4250e+06
Rg (reciprocal space) rg_reciprocal34.24
I(0) (reciprocal space) i0_reciprocal212700000.0000
Solution quality estimate total_estimate0.8703
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.444
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49910000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)