Research workbench
AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase (P00497)
Analyse AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase (P00497) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P00497
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Amidophosphoribosyltransferase
- UniProt
- P00497
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidophosphoribosyltransferase | protein | 476 | 32% helix, 24% strand | P00497 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.80 | 0.97 | 23 | empty |
| 2 | 933 | 0.77 | 0.80 | 73 | empty |
| 3 | 114 | 0.41 | 0.76 | 16 | empty |
| 4 | 80 | 0.37 | 0.77 | 19 | empty |
Compared structures
- 1GPH · Structure of the allosteric regulatory enzyme of purine biosynthesis · an experimental structure of the same protein · chain A against 1, TM-score 0.96
- 1GPH · Structure of the allosteric regulatory enzyme of purine biosynthesis · an experimental structure of the same protein · chain A against 1, TM-score 0.96
- 1AO0 · Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from B. subtilis complexed… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 1AO0 · Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from B. subtilis complexed… · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 P00497
- Elsewhere: UniProt P00497 · AlphaFold DB P00497
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