MolNFT v1 · #502042 · protein
AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (A1D4E3)
A1D4E3: “AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (A1D4E3)”. 2 pockets (best druggability 0.70). MolNFT v1 #502042 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A1D4E3
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Probable NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- A1D4E3
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NAD(P)H-dependent D-xylose reductase XYL1 | protein | 321 | 41% helix, 15% strand | A1D4E3 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 358 | 0.70 | 0.83 | 52 | empty |
| 2 | 58 | 0.30 | 0.75 | 20 | empty |
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 A1D4E3
- Elsewhere: UniProt A1D4E3 · AlphaFold DB A1D4E3
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