Research workbench
AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine cyclo-ligase (O58054)
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
- O58054
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x245Fa93d080F0Ea0899525993BC10b55e79b454D
- Molecule
- Phosphoribosylformylglycinamidine cyclo-ligase
- UniProt
- O58054
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylformylglycinamidine cyclo-ligase | protein | 334 | 37% helix, 25% strand | O58054 |
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 | 180 | 0.42 | 0.73 | 27 | empty |
| 2 | 69 | 0.31 | 0.74 | 17 | empty |
| 3 | 51 | 0.28 | 0.75 | 12 | 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 O58054
- Elsewhere: UniProt O58054 · AlphaFold DB O58054
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