Research workbench
AlphaFold monomer V2.0 prediction for N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (Q89WE6)
Analyse AlphaFold monomer V2.0 prediction for N-(5'-PHOSPHORIBOSYL)ANTHRANILATE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q89WE6
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase
- UniProt
- Q89WE6
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase | protein | 223 | 39% helix, 21% strand | Q89WE6 |
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 | 65 | 0.69 | 0.96 | 32 | empty |
| 2 | 63 | 0.30 | 0.74 | 16 | 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 Q89WE6
- Elsewhere: UniProt Q89WE6 · AlphaFold DB Q89WE6
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