7s15

GLP-1 receptor bound with Pfizer small molecule agonist

Method: ELECTRON MICROSCOPY Dmax: 104.3 Å Quality: GOOD

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

Glucagon-like peptide 1 receptor

Homo sapiens

UniProt P43220

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain R; UniProt 24–422 Mutation:I146Y, A208R, Q213E, S219R, L260A, Y291A, L339E, K346Q 82L 2-[(4-{6-[(2,4-difluorophenyl)methoxy]pyridin-2-yl}piperidin-1-yl)methyl]-1-[(1-ethyl-1H-imidazol-5-yl)methyl]-1H-benzimidazole-6-carboxylic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;-2 blotting force 4S blotting time Resolution 3.80 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.

69 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLP1R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–399; UniProt 24–422

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 7s15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s15
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7s15
Deposition date deposition_date2021-09-01
Structure title titleGLP-1 receptor bound with Pfizer small molecule agonist
Keywords keywordsGLP-1R, GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.61
Radius of gyration Rg (electron density) rg_electron28.99
Forward intensity I(0) i030308400.00
Molecular weight molecular_weight45296.0 kDa
Excluded volume excluded_volume57785 ų
Envelope volume envelope_volume77172 ų
Hydration-shell volume shell_volume24758 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg32.51
Envelope Rg envelope_rg29.93
Shape Rg shape_rg28.97
Total Rg total_rg29.48
Total atoms total_atoms3207
Residues n_residues382
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 dmax104.3
Rg (real space) rg_real30.03
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real3.0310e+07
I(0) uncertainty (real space) i0_real_error5.1360e+05
Rg (reciprocal space) rg_reciprocal29.85
I(0) (reciprocal space) i0_reciprocal30300000.0000
Solution quality estimate total_estimate0.7877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.650
Kurtosis Kurtosis kurtosis-0.201
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5547000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.609; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.586; Smooth: 0.822

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7s15R01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)