MolNFT v1 · #154747 · protein
Beta-arrestin 1 mutant S13D/T275D
6KL7 · Beta-arrestin-1: “Beta-arrestin 1 mutant S13D/T275D”. X-ray diffraction, 1 ligand (BA), 8 pockets (best druggability 0.65). MolNFT v1 #154747 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KL7
- Type
- protein
- Length
- 685 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-arrestin-1
- UniProt
- P29066
- Ligands
- BA
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-arrestin-1 | protein | 355 | 5% helix, 49% strand | P29066 |
| B | Beta-arrestin-1 | protein | 330 | 3% helix, 49% strand | P29066 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.65 | 0.94 | 21 | empty |
| 2 | 377 | 0.60 | 0.77 | 50 | empty |
| 3 | 97 | 0.46 | 0.80 | 21 | empty |
| 4 | 90 | 0.42 | 0.78 | 25 | empty |
| 5 | 59 | 0.30 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 746 Ų buried · 15 hydrogen bonds · protein-protein
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 P29066
- Elsewhere: RCSB PDB 6KL7 · PDBe 6KL7 · UniProt P29066
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