Research workbench
Structure of the class B human glucagon G protein coupled receptor
Analyse Structure of the class B human glucagon G protein coupled receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L6R
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble cytochrome B562 and glucagon receptor chimera
- UniProt
- P0ABE7, P47871
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble cytochrome B562 and glucagon receptor chimera | protein | 398 | 73% helix, 0% strand | P0ABE7, P47871 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.74 | 0.79 | 73 | empty |
| 2 | 71 | 0.48 | 0.83 | 14 | empty |
| 3 | 53 | 0.39 | 0.81 | 15 | PEG |
| 4 | 65 | 0.35 | 0.77 | 18 | empty |
| 5 | 68 | 0.27 | 0.72 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4L6R · Structure of the class B human glucagon G protein coupled receptor · the same entry in another collection · chain A against A, TM-score 1.00
- P47871 · AlphaFold monomer V2.0 prediction for glucagon receptor (P47871) · a predicted model of the same protein · chain A against A, TM-score 0.65
- P0ABE7 · AlphaFold monomer V2.0 prediction for soluble cytochrome B562 (P0ABE7) · a predicted model of the same protein · chain A against A, TM-score 0.26
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 P0ABE7
- Every structure of UniProt P47871
- Elsewhere: RCSB PDB 4L6R · PDBe 4L6R · UniProt P0ABE7 · UniProt P47871
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