Research workbench
AlphaFold monomer V2.0 prediction for N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (P12289)
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
- P12289
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x629e2743E9cB912e911eF9394Ab0f16Acc3A5f5c
- Molecule
- N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase
- UniProt
- P12289
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase | protein | 219 | 36% helix, 22% strand | P12289 |
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 | 97 | 0.75 | 0.97 | 31 | empty |
| 2 | 64 | 0.27 | 0.73 | 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 P12289
- Elsewhere: UniProt P12289 · AlphaFold DB P12289
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