Research workbench
AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine cyclo-ligase (Q2P674)
Analyse AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2P674
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc2C3F148eB26FE91165F4EE55FE4D2E3738B0950
- Molecule
- Phosphoribosylformylglycinamidine cyclo-ligase
- UniProt
- Q2P674
- Pockets
- 3 · best druggability 0.49
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylformylglycinamidine cyclo-ligase | protein | 341 | 36% helix, 24% strand | Q2P674 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.49 | 0.79 | 24 | empty |
| 2 | 73 | 0.33 | 0.75 | 17 | empty |
| 3 | 64 | 0.33 | 0.76 | 15 | 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 Q2P674
- Elsewhere: UniProt Q2P674 · AlphaFold DB Q2P674
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