Research workbench
Crystal of ARRESTIN2-V2RPP-1-FAB30 complex
Analyse Crystal of ARRESTIN2-V2RPP-1-FAB30 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DF9
- Type
- protein
- Length
- 800 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-arrestin-1; Vasopressin V2 receptor phosphopeptide; FAB30 light chain; FAB30 heavy…
- UniProt
- P17870
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-arrestin-1 | protein | 360 | 6% helix, 43% strand | P17870 |
| V | Vasopressin V2 receptor phosphopeptide | protein | 20 | 0% helix, 20% strand | — |
| L | FAB30 light chain | protein | 212 | 5% helix, 39% strand | — |
| H | FAB30 heavy chain | protein | 208 | 3% helix, 41% strand | — |
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 | 1080 | 0.80 | 0.81 | 105 | empty |
| 2 | 140 | 0.64 | 0.88 | 31 | empty |
| 3 | 287 | 0.55 | 0.76 | 41 | empty |
| 4 | 106 | 0.55 | 0.84 | 32 | empty |
| 5 | 280 | 0.51 | 0.74 | 36 | empty |
Interfaces
5 interfaces between chains.
- L–H · 1663 Ų buried · 9 hydrogen bonds · protein-protein
- A–V · 1007 Ų buried · 22 hydrogen bonds · protein-protein
- A–H · 695 Ų buried · 6 hydrogen bonds · protein-protein
- A–L · 331 Ų buried · 1 hydrogen bond · protein-protein
- V–L · 95 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified, 4 disulfide (phosphorylation, disulfide).
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 P17870
- Elsewhere: RCSB PDB 7DF9 · PDBe 7DF9 · UniProt P17870
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