Research workbench
AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine cyclo-ligase (C3L534)
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
- C3L534
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7E98f6A02556dc8C8E41BFbaE3d5CEB7162e02a2
- Molecule
- Phosphoribosylformylglycinamidine cyclo-ligase
- UniProt
- C3L534
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylformylglycinamidine cyclo-ligase | protein | 346 | 36% helix, 24% strand | C3L534 |
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 | 195 | 0.53 | 0.78 | 31 | empty |
| 2 | 165 | 0.48 | 0.77 | 30 | empty |
| 3 | 73 | 0.32 | 0.75 | 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 C3L534
- Elsewhere: UniProt C3L534 · AlphaFold DB C3L534
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