MolNFT v1 · #164399 · protein
Crystal structure of the tasor-periphilin core complex
6SWG · Periphilin-1: “Crystal structure of the tasor-periphilin core complex”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.29). MolNFT v1 #164399 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6SWG
- Type
- protein
- Length
- 209 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periphilin-1; Protein tasor
- UniProt
- Q8NEY8, Q9UK61
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 3 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periphilin-1 | protein | 72 | 88% helix, 0% strand | Q8NEY8 |
| B | Periphilin-1 | protein | 74 | 95% helix, 0% strand | Q8NEY8 |
| C | Protein tasor | protein | 63 | 63% helix, 0% strand | Q9UK61 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.29 | 0.74 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1319 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 804 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 796 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6SWG · Crystal structure of the TASOR-Periphilin core complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NEY8 · AlphaFold monomer V2.0 prediction for periphilin-1 (Q8NEY8) · a predicted model of the same protein · chain B against A, TM-score 0.62
- Q9UK61 · AlphaFold monomer V2.0 prediction for protein tasor (Q9UK61) · a predicted model of the same protein · chain C against A, TM-score 0.54
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 Q8NEY8
- Every structure of UniProt Q9UK61
- Elsewhere: RCSB PDB 6SWG · PDBe 6SWG · UniProt Q8NEY8 · UniProt Q9UK61
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