MolNFT v1 · #117871 · protein
The structure of DHAR1 from arabidopsis thaliana
5EL8 · Glutathione S-transferase DHAR1, mitochondrial: “The structure of DHAR1 from arabidopsis thaliana”. X-ray diffraction, 2 pockets (best druggability 0.41). MolNFT v1 #117871 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5EL8
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase DHAR1, mitochondrial
- EC
- 2.5.1.18, 1.8.5.1
- UniProt
- Q9FWR4
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase DHAR1, mitochondrial (EC 2.5.1.18, 1.8.5.1) | protein | 213 | 48% helix, 13% strand | Q9FWR4 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.41 | 0.79 | 25 | empty |
| 2 | 75 | 0.33 | 0.74 | 15 | GOL |
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 Q9FWR4
- Elsewhere: RCSB PDB 5EL8 · PDBe 5EL8 · UniProt Q9FWR4
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