3c5t

Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain

Method: X-RAY DIFFRACTION Dmax: 65.0 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 24–145 Fragment:N-terminal extracellular domain, UNP residues 24-145 Exendin-4 × 1 (P26349) 10M decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.1M Tris-HCl pH 8.5, 0.1M MgCl2, 0.4M MgTartrate, 9mM n-Decyl-beta-D-thiomaltoside, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 Å R-free 0.238

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 A; PDBConstruct 1–122; UniProt 24–145

Exendin-4

OrganismNot specified

UniProt P26349

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 B; UniProt 56–86 Fragment:UNP residues 56-86 Glucagon-like peptide 1 receptor × 1 (P43220) 10M decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.1M Tris-HCl pH 8.5, 0.1M MgCl2, 0.4M MgTartrate, 9mM n-Decyl-beta-D-thiomaltoside, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 Å R-free 0.238

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXE4_HELSU
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–31; UniProt 56–86

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 3c5t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3c5t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3c5t
Deposition date deposition_date2008-02-01
Structure title titleCrystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
Keywords keywords;ligand-bound G protein-coupled receptor extracellular domain, G-protein coupled receptor, Glycoprotein, Membrane, Transducer, Transmembrane, Amidation, Cleavage on pair of basic residues, Secreted, Signaling protein-Signaling protein COMPLEX ;; 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_guinier16.91
Radius of gyration Rg (electron density) rg_electron16.06
Forward intensity I(0) i04868860.00
Molecular weight molecular_weight15459.0 kDa
Excluded volume excluded_volume19152 ų
Envelope volume envelope_volume23035 ų
Hydration-shell volume shell_volume12681 ų
Envelope diameter envelope_diameter63.2
Shell Rg shell_rg21.33
Envelope Rg envelope_rg16.54
Shape Rg shape_rg16.01
Total Rg total_rg17.21
Total atoms total_atoms1088
Residues n_residues129
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 dmax65.0
Rg (real space) rg_real16.92
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.8690e+06
I(0) uncertainty (real space) i0_real_error5.8540e+04
Rg (reciprocal space) rg_reciprocal16.92
I(0) (reciprocal space) i0_reciprocal4869000.0000
Solution quality estimate total_estimate0.8040
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.420
Kurtosis Kurtosis kurtosis0.074
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha688100.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.536; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.839; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3c5tb1
Class classj — Peptides
Fold Fold foldj.6 — Peptide hormones
Superfamily Superfamily superfamilyj.6.1 — Peptide hormones
Family Family familyj.6.1.1 — Peptide hormones

CATH v4.4 (1 domains)

Domain ID domain_id3c5tA00
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)