Research workbench
AlphaFold monomer V2.0 prediction for formate-dependent phosphoribosylglycinamide formyltransferase (Q1H1W4)
Analyse AlphaFold monomer V2.0 prediction for formate-dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1H1W4
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFEC3770b1Fd39BD2C1bEe43e6a8614DE7ACf0eF5
- Molecule
- Formate-dependent phosphoribosylglycinamide formyltransferase
- UniProt
- Q1H1W4
- Pockets
- 2 · best druggability 0.80
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate-dependent phosphoribosylglycinamide formyltransferase | protein | 400 | 34% helix, 30% strand | Q1H1W4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 728 | 0.80 | 0.84 | 71 | empty |
| 2 | 83 | 0.33 | 0.74 | 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 Q1H1W4
- Elsewhere: UniProt Q1H1W4 · AlphaFold DB Q1H1W4
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