Research workbench
AlphaFold monomer V2.0 prediction for GTP cyclohydrolase-2 (A0RR75)
Analyse AlphaFold monomer V2.0 prediction for GTP cyclohydrolase-2 (A0RR75) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0RR75
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x98cF31c0D697544FB4BdA74FB5Eb926d2aE4D74b
- Molecule
- GTP cyclohydrolase-2
- UniProt
- A0RR75
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP cyclohydrolase-2 | protein | 195 | 35% helix, 25% strand | A0RR75 |
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 | 167 | 0.79 | 0.95 | 30 | empty |
| 2 | 95 | 0.35 | 0.73 | 17 | empty |
| 3 | 65 | 0.31 | 0.75 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A0RR75
- Elsewhere: UniProt A0RR75 · AlphaFold DB A0RR75
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