Research workbench
A high-resolution cryo-electron microscopy structure of a calcitonin receptor-heterotrimeric gs protein complex
Analyse A high-resolution cryo-electron microscopy structure of a calcitonin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NIY
- Type
- protein
- Length
- 965 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; NANOBODY35…
- UniProt
- P63092, P30988, P62873, P59768, Q92163
- Pockets
- 11 · best druggability 0.84
Structure
electron microscopy · 6 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 168 | 46% helix, 20% strand | P63092 |
| N | NANOBODY35 | protein | 128 | 2% helix, 45% strand | — |
| R | Calcitonin receptor | protein | 261 | 83% helix, 0% strand | P30988 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 334 | 8% helix, 46% strand | P62873 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 55 | 55% helix, 0% strand | P59768 |
| P | Calcitonin | protein | 19 | 74% helix, 5% strand | Q92163 |
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 | 866 | 0.84 | 0.86 | 95 | empty |
| 2 | 783 | 0.72 | 0.78 | 46 | empty |
| 3 | 792 | 0.72 | 0.77 | 64 | empty |
| 4 | 52 | 0.68 | 0.97 | 18 | empty |
| 5 | 219 | 0.60 | 0.81 | 38 | empty |
Interfaces
7 interfaces between chains.
- B–G · 2185 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1552 Ų buried · 20 hydrogen bonds · protein-protein
- R–P · 1236 Ų buried · 10 hydrogen bonds · protein-protein
- A–R · 1092 Ų buried · 13 hydrogen bonds · protein-protein
- A–N · 761 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6NIY · A high-resolution cryo-electron microscopy structure of a calcitonin… · the same entry in another collection · chain P against P, 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
- P30988 · AlphaFold monomer V2.0 prediction for calcitonin receptor (P30988) · a predicted model of the same protein · chain R against A, TM-score 0.96
- 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 G against A, TM-score 0.93
- 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 0.81
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 P30988
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Every structure of UniProt Q92163
- Elsewhere: RCSB PDB 6NIY · PDBe 6NIY · UniProt P63092 · UniProt P30988 · UniProt P62873 · UniProt P59768 · UniProt Q92163
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