MolNFT v1 · #61818 · protein
Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form
3DWV · Glutathione peroxidase-like protein: “Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form”. X-ray diffraction, 5 pockets (best druggability 0.54). MolNFT v1 #61818 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3DWV
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione peroxidase-like protein
- EC
- 1.11.1.9
- UniProt
- Q869A5
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione peroxidase-like protein (EC 1.11.1.9) | protein | 163 | 28% helix, 20% strand | Q869A5 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.54 | 0.79 | 36 | empty |
| 2 | 131 | 0.49 | 0.79 | 25 | empty |
| 3 | 85 | 0.38 | 0.77 | 16 | empty |
| 4 | 113 | 0.35 | 0.73 | 22 | empty |
| 5 | 66 | 0.31 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 641 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3DWV · Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form · 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 Q869A5
- Elsewhere: RCSB PDB 3DWV · PDBe 3DWV · UniProt Q869A5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.