MolNFT v1 · #176222 · protein
Crystal of ARRESTIN2-V2RPP-3-FAB30 complex
7DFC · Beta-arrestin-1: “Crystal of ARRESTIN2-V2RPP-3-FAB30 complex”. X-ray diffraction, 11 pockets (best druggability 0.81). MolNFT v1 #176222 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DFC
- Type
- protein
- Length
- 799 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-arrestin-1; V2RPP-3; FAB30 light chain; FAB30 heavy chain
- UniProt
- P17870
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-arrestin-1 | protein | 359 | 4% helix, 47% strand | P17870 |
| V | V2RPP-3 | protein | 19 | 0% helix, 37% strand | — |
| L | FAB30 light chain | protein | 211 | 5% helix, 50% strand | — |
| H | FAB30 heavy chain | protein | 210 | 4% helix, 54% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.81 | 0.92 | 47 | empty |
| 2 | 657 | 0.72 | 0.79 | 62 | empty |
| 3 | 283 | 0.57 | 0.77 | 47 | empty |
| 4 | 159 | 0.57 | 0.82 | 36 | empty |
| 5 | 359 | 0.54 | 0.74 | 58 | empty |
Interfaces
5 interfaces between chains.
- L–H · 1623 Ų buried · 13 hydrogen bonds · protein-protein
- A–V · 1235 Ų buried · 32 hydrogen bonds · protein-protein
- A–H · 710 Ų buried · 6 hydrogen bonds · protein-protein
- A–L · 333 Ų buried · 7 hydrogen bonds · protein-protein
- V–L · 105 Ų buried · 3 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 7DFC · PDBe 7DFC · UniProt P17870
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