Research workbench
Cryoem structure of gq-coupled MRGPRX2 with peptide agonist cortistatin-14
Analyse Cryoem structure of gq-coupled MRGPRX2 with peptide agonist cortistatin-14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S8L
- Type
- protein
- Length
- 1,096 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mas-related G-protein coupled receptor member X2; Cortistatin 14; Gs-mini-gq chimera…
- UniProt
- Q96LB1, P62873, P59768
- Pockets
- 13 · best druggability 0.82
Structure
electron microscopy · 6 distinct chains · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | Mas-related G-protein coupled receptor member X2 | protein | 250 | 82% helix, 0% strand | Q96LB1 |
| A | Cortistatin 14 | protein | 6 | 0% helix, 0% strand | — |
| B | Gs-mini-gq chimera | protein | 221 | 47% helix, 17% strand | — |
| C | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 337 | 7% helix, 47% strand | P62873 |
| D | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 51 | 57% helix, 0% strand | P59768 |
| E | SCFV16 | protein | 231 | 3% helix, 45% strand | — |
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 911 | 0.82 | 0.84 | 66 | empty |
| 2 | 566 | 0.68 | 0.78 | 59 | empty |
| 3 | 70 | 0.64 | 0.92 | 15 | empty |
| 4 | 545 | 0.64 | 0.75 | 54 | empty |
| 5 | 107 | 0.54 | 0.84 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1991 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1042 Ų buried · 9 hydrogen bonds · protein-protein
- R–B · 942 Ų buried · 6 hydrogen bonds · protein-protein
- R–A · 655 Ų buried · 6 hydrogen bonds · protein-protein
- B–E · 531 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7S8L · CryoEM structure of Gq-coupled MRGPRX2 with peptide agonist Cortistatin-14 · 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 C against A, TM-score 0.99
- Q96LB1 · AlphaFold monomer V2.0 prediction for mas-related G-protein coupled receptor member X2… · a predicted model of the same protein · chain R against A, TM-score 0.95
- 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 D against A, TM-score 0.85
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 Q96LB1
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Elsewhere: RCSB PDB 7S8L · PDBe 7S8L · UniProt Q96LB1 · UniProt P62873 · UniProt P59768
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