Research workbench
Structure and mode of peptide binding of pheromone receptor prgz
Analyse Structure and mode of peptide binding of pheromone receptor prgz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FAJ
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prgz; Sex pheromone CCF10
- UniProt
- Q51643, P20104
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prgz | protein | 507 | 32% helix, 23% strand | Q51643 |
| B | Sex pheromone CCF10 | protein | 7 | 0% helix, 29% strand | P20104 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.82 | 0.96 | 36 | empty |
| 2 | 511 | 0.75 | 0.83 | 70 | GOL |
| 3 | 189 | 0.46 | 0.75 | 29 | empty |
| 4 | 64 | 0.34 | 0.77 | 18 | empty |
| 5 | 86 | 0.33 | 0.73 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4FAJ · Structure and mode of peptide binding of pheromone receptor PrgZ · the same entry in another collection · chain A against A, TM-score 1.00
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 Q51643
- Every structure of UniProt P20104
- Elsewhere: RCSB PDB 4FAJ · PDBe 4FAJ · UniProt Q51643 · UniProt P20104
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