MolNFT v1 · #11895 · protein
URE2P in complex with S-hexylglutathione
1K0A · URE2 protein: “URE2P in complex with S-hexylglutathione”. X-ray diffraction, 2 ligands (GTX, GSH), 6 pockets (best druggability 0.72). MolNFT v1 #11895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1K0A
- Type
- protein
- Length
- 457 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- URE2 protein
- UniProt
- P23202
- Ligands
- GTX, GSH
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | URE2 protein | protein | 234 | 62% helix, 8% strand | P23202 |
| B | URE2 protein | protein | 223 | 59% helix, 9% strand | P23202 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 529 | 0.72 | 0.80 | 40 | GSH |
| 2 | 544 | 0.70 | 0.79 | 36 | GTX |
| 3 | 171 | 0.58 | 0.82 | 26 | empty |
| 4 | 91 | 0.36 | 0.75 | 19 | empty |
| 5 | 77 | 0.33 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1883 Ų buried · 25 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 P23202
- Elsewhere: RCSB PDB 1K0A · PDBe 1K0A · UniProt P23202
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.