5otv

Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cyc/Thr11Hcs

Method: X-RAY DIFFRACTION Dmax: 68.7 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 24–139 Fragment:extracellular domain, UNP residues 24-139 Glucagon × 1 (P01275) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000 Resolution 2.00 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 24–139 Fragment:extracellular domain, UNP residues 24-139 Glucagon × 1 (P01275) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000 Resolution 2.00 Å R-free 0.246

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 78 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 A; PDBConstruct 1–116; UniProt 24–139 Author chain C; PDBConstruct 1–116; UniProt 24–139

Glucagon

OrganismNot specified

UniProt P01275

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 98–128 Mutation:A8C, T11HCS Non-standard monomer:Yes (specific site not provided by mmCIF) Glucagon-like peptide 1 receptor × 1 (P43220) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000 Resolution 2.00 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 98–128 Mutation:A8C, T11HCS Non-standard monomer:Yes (specific site not provided by mmCIF) Glucagon-like peptide 1 receptor × 1 (P43220) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000 Resolution 2.00 Å R-free 0.246

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.

33 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLUC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–31; UniProt 98–128 Author chain D; PDBConstruct 1–31; UniProt 98–128

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 5otv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5otv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5otv
Deposition date deposition_date2017-08-22
Structure title titleExtracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cyc/Thr11Hcs
Keywords keywordsglucagon-like peptide 1, GPCR, cyclic peptides, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.37
Radius of gyration Rg (electron density) rg_electron21.56
Forward intensity I(0) i016103600.00
Molecular weight molecular_weight29514.0 kDa
Excluded volume excluded_volume36510 ų
Envelope volume envelope_volume49075 ų
Hydration-shell volume shell_volume19595 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg27.44
Envelope Rg envelope_rg21.51
Shape Rg shape_rg21.52
Total Rg total_rg22.49
Total atoms total_atoms2084
Residues n_residues256
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 dmax68.7
Rg (real space) rg_real22.28
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.6100e+07
I(0) uncertainty (real space) i0_real_error2.1660e+05
Rg (reciprocal space) rg_reciprocal22.30
I(0) (reciprocal space) i0_reciprocal16100000.0000
Solution quality estimate total_estimate0.9151
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.126
Kurtosis Kurtosis kurtosis-0.609
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1288000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5otvA01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology1240 — Hormone receptor fold
Homologous superfamily homologous superfamily10 — GPCR, family 2, extracellular hormone receptor domain
Domain ID domain_id5otvC01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology1240 — Hormone receptor fold
Homologous superfamily homologous superfamily10 — GPCR, family 2, extracellular hormone receptor domain

8. Citations (1)

9. Files and Curves (10)