Research workbench
Tethered peptide activation mechanism of adhesion gpcrs ADGRG2 and ADGRG4
Analyse Tethered peptide activation mechanism of adhesion gpcrs ADGRG2 and ADGRG4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WUJ
- Type
- protein
- Length
- 1,209 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mini-gs; Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1; Adhesion…
- UniProt
- P62873, Q8IZF6, P59768
- Pockets
- 12 · best druggability 0.79
Structure
electron microscopy · 6 distinct chains · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mini-gs | protein | 233 | 41% helix, 13% strand | — |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 334 | 6% helix, 43% strand | P62873 |
| E | Adhesion G-protein coupled receptor G4,UNCHARACTERIZED protein | protein | 267 | 70% helix, 0% strand | Q8IZF6 |
| S | SCFV16 | protein | 222 | 1% helix, 35% strand | — |
| Y | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 56 | 39% helix, 0% strand | P59768 |
| N | Nanobody-35 | protein | 97 | 3% helix, 34% strand | — |
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.79 | 0.87 | 54 | empty |
| 2 | 974 | 0.74 | 0.77 | 70 | empty |
| 3 | 709 | 0.71 | 0.78 | 50 | empty |
| 4 | 603 | 0.68 | 0.77 | 71 | empty |
| 5 | 98 | 0.59 | 0.87 | 24 | empty |
Interfaces
8 interfaces between chains.
- B–Y · 1824 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1503 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 1125 Ų buried · 11 hydrogen bonds · protein-protein
- A–N · 675 Ų buried · 3 hydrogen bonds · protein-protein
- A–S · 602 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7WUJ · Tethered peptide activation mechanism of adhesion GPCRs ADGRG2 and ADGRG4 · the same entry in another collection · chain N against N, 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 0.98
- 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 Y against A, TM-score 0.86
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 P62873
- Every structure of UniProt Q8IZF6
- Every structure of UniProt P59768
- Elsewhere: RCSB PDB 7WUJ · PDBe 7WUJ · UniProt P62873 · UniProt Q8IZF6 · UniProt P59768
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