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Structure of the ligand-free GPCR dimer STE2
Analyse Structure of the ligand-free GPCR dimer STE2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QB9
- Type
- protein
- Length
- 598 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pheromone alpha factor receptor
- UniProt
- P0CI39
- Ligands
- Y01, NAG
- Pockets
- 7 · best druggability 0.73
Structure
electron microscopy · 1 distinct chain · 67% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pheromone alpha factor receptor | protein | 299 | 67% helix, 4% strand | P0CI39 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 22 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 725 | 0.73 | 0.79 | 61 | empty |
| 2 | 750 | 0.72 | 0.78 | 65 | empty |
| 3 | 441 | 0.63 | 0.76 | 42 | Y01 |
| 4 | 306 | 0.55 | 0.75 | 25 | Y01 |
| 5 | 96 | 0.41 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2256 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 glycan (N-glycosylation).
Compared structures
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 P0CI39
- Elsewhere: RCSB PDB 7QB9 · PDBe 7QB9 · UniProt P0CI39
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