3c5t

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

Method: X-RAY DIFFRACTION
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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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Exendin-4 × 1 (P26349) decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Glucagon-like peptide 1 receptor × 1 (P43220) decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

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.

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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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3c5t__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3c5t__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3c5t__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)16.91 Å
Rg (electron density)16.06 Å
Total Rg17.21 Å
Atom count1088
Residues129
Excluded volume19152 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3c5t__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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6. 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
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7. Citations (1)