MolNFT v1 · #92133 · protein
Crystal structure of leut-F253A bound to L-selenomethionine from lipid bicelles
4FY0 · Transporter: “Crystal structure of leut-F253A bound to L-selenomethionine from lipid bicelles”. X-ray diffraction, 2 ligands (MSE, NA), 4 pockets (best druggability 0.75). MolNFT v1 #92133 on GenesisL1: 3D structure, binding sites…
- PDB
- 4FY0
- Type
- protein
- Length
- 502 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transporter
- UniProt
- O67854
- Ligands
- MSE, NA
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transporter | protein | 502 | 78% helix, 1% strand | O67854 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.75 | 0.80 | 69 | MSE |
| 2 | 68 | 0.52 | 0.86 | 15 | empty |
| 3 | 105 | 0.45 | 0.78 | 15 | empty |
| 4 | 106 | 0.37 | 0.73 | 10 | empty |
Compared structures
- 4FY0 · Crystal structure of LeuT-F253A bound to L-selenomethionine from lipid bicelles · 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 O67854
- Elsewhere: RCSB PDB 4FY0 · PDBe 4FY0 · UniProt O67854
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.