Research workbench
Cryo-EM structure of the human glucagon receptor in complex with gs
Analyse Cryo-EM structure of the human glucagon receptor in complex with gs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LMK
- Type
- protein
- Length
- 1,178 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(S) subunit alpha isoforms short; Guanine…
- UniProt
- P63092, P62873, P59768, P47871, P01275
- Pockets
- 16 · best druggability 0.80
Structure
electron microscopy · 6 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 231 | 43% helix, 17% strand | P63092 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 339 | 8% helix, 41% strand | P62873 |
| C | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 56 | 54% helix, 0% strand | P59768 |
| N | NB35 | protein | 128 | 5% helix, 39% strand | — |
| R | Glucagon receptor | protein | 395 | 57% helix, 5% strand | P47871 |
| E | Glucagon | protein | 29 | 86% helix, 0% strand | P01275 |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.80 | 0.86 | 48 | empty |
| 2 | 910 | 0.74 | 0.78 | 60 | empty |
| 3 | 706 | 0.71 | 0.78 | 46 | empty |
| 4 | 144 | 0.65 | 0.87 | 25 | empty |
| 5 | 195 | 0.62 | 0.83 | 38 | empty |
Interfaces
7 interfaces between chains.
- B–C · 2097 Ų buried · 17 hydrogen bonds · protein-protein
- R–E · 2012 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1518 Ų buried · 14 hydrogen bonds · protein-protein
- A–R · 1343 Ų buried · 12 hydrogen bonds · protein-protein
- A–N · 962 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6LMK · Cryo-EM structure of the human glucagon receptor in complex with Gs · the same entry in another collection · chain E against E, 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 0.97
- 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 0.91
- P63092 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(S) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.84
- P01275 · AlphaFold monomer V2.0 prediction for pro-glucagon (P01275) · a predicted model of the same protein · chain E against A, TM-score 0.79
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 P63092
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Every structure of UniProt P47871
- Every structure of UniProt P01275
- Elsewhere: RCSB PDB 6LMK · PDBe 6LMK · UniProt P63092 · UniProt P62873 · UniProt P59768 · UniProt P47871 · UniProt P01275
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.