MolNFT v1 · #116317 · protein
Dehydroascorbate reductase (osdhar) complexed with asa
5D9W: “Dehydroascorbate reductase (osdhar) complexed with asa”. X-ray diffraction, 1 ligand (ASC), 2 pockets (best druggability 0.39). MolNFT v1 #116317 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5D9W
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dehydroascorbate reductase
- UniProt
- Q65XA0
- Ligands
- ASC
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dehydroascorbate reductase | protein | 211 | 53% helix, 13% strand | Q65XA0 |
Ligands and binding sites
- ASC · Ascorbic acid · ligand · 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 | 94 | 0.39 | 0.77 | 23 | empty |
| 2 | 71 | 0.33 | 0.75 | 16 | ASC |
Compared structures
- Q65XA0 · AlphaFold monomer V2.0 prediction for probable glutathione S-transferase DHAR1, cytosolic… · a predicted model of the same protein · 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 Q65XA0
- Elsewhere: RCSB PDB 5D9W · PDBe 5D9W · UniProt Q65XA0
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