Research workbench
Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
Analyse Crystal structure of the ligand-bound glucagon-like peptide-1 receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C59
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucagon-like peptide 1 receptor; Exendin-4
- UniProt
- P43220, P26349
- Ligands
- 10M
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucagon-like peptide 1 receptor | protein | 103 | 26% helix, 19% strand | P43220 |
| B | Exendin-4 | protein | 27 | 67% helix, 0% strand | P26349 |
Ligands and binding sites
- 10M · decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.28 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 698 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 2 modified (disulfide, engineered).
Compared structures
- 3C59 · Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular… · the same entry in another collection · chain A against A, TM-score 1.00
- P43220 · AlphaFold monomer V2.0 prediction for glucagon-like peptide 1 receptor (P43220) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P26349 · AlphaFold monomer V2.0 prediction for exendin-4 (P26349) · a predicted model of the same protein · chain B against A, TM-score 0.80
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P43220
- Every structure of UniProt P26349
- Elsewhere: RCSB PDB 3C59 · PDBe 3C59 · UniProt P43220 · UniProt P26349
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