Research workbench
AlphaFold monomer V2.0 prediction for GTP cyclohydrolase-2 (A4Y5N5)
Analyse AlphaFold monomer V2.0 prediction for GTP cyclohydrolase-2 (A4Y5N5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4Y5N5
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x16633532dE8F3b41E31C55a2AB62808E315CeDCC
- Molecule
- GTP cyclohydrolase-2
- UniProt
- A4Y5N5
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP cyclohydrolase-2 | protein | 203 | 34% helix, 27% strand | A4Y5N5 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.74 | 0.90 | 39 | empty |
| 2 | 70 | 0.32 | 0.74 | 13 | empty |
| 3 | 54 | 0.28 | 0.75 | 14 | 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 A4Y5N5
- Elsewhere: UniProt A4Y5N5 · AlphaFold DB A4Y5N5
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