Research workbench
Cryo-EM structure of the human glucagon receptor in complex with GI1
Analyse Cryo-EM structure of the human glucagon receptor in complex with GI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LML
- Type
- protein
- Length
- 1,219 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I) subunit alpha-1; Guanine nucleotide-binding…
- UniProt
- P63096, P62873, P59768, P01275, P47871
- Pockets
- 11 · best druggability 0.82
Structure
electron microscopy · 6 distinct chains · 27% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(I) subunit alpha-1 | protein | 224 | 36% helix, 12% strand | P63096 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 306 | 0% helix, 36% strand | P62873 |
| C | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 33 | 48% helix, 0% strand | P59768 |
| D | SCFV16 | protein | 232 | 3% helix, 36% strand | — |
| E | Glucagon | protein | 29 | 83% helix, 0% strand | P01275 |
| R | Glucagon receptor | protein | 395 | 52% helix, 3% strand | P47871 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 622 | 0.82 | 0.87 | 55 | empty |
| 2 | 697 | 0.70 | 0.77 | 63 | empty |
| 3 | 373 | 0.64 | 0.79 | 56 | empty |
| 4 | 191 | 0.53 | 0.78 | 31 | empty |
| 5 | 131 | 0.51 | 0.80 | 23 | empty |
Interfaces
7 interfaces between chains.
- E–R · 2149 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1360 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1071 Ų buried · 4 hydrogen bonds · protein-protein
- A–R · 767 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 534 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6LML · Cryo-EM structure of the human glucagon receptor in complex with Gi1 · the same entry in another collection · chain R against R, TM-score 1.00
- P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P47871 · AlphaFold monomer V2.0 prediction for glucagon receptor (P47871) · a predicted model of the same protein · chain R against A, TM-score 0.95
- P63096 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.83
- P01275 · AlphaFold monomer V2.0 prediction for pro-glucagon (P01275) · a predicted model of the same protein · chain E against A, TM-score 0.75
- P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain C against A, TM-score 0.71
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 P63096
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Every structure of UniProt P01275
- Every structure of UniProt P47871
- Elsewhere: RCSB PDB 6LML · PDBe 6LML · UniProt P63096 · UniProt P62873 · UniProt P59768 · UniProt P01275 · UniProt P47871
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