Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (Q1I5K9)
Analyse AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1I5K9
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Gmp synthase [glutamine-hydrolyzing]
- UniProt
- Q1I5K9
- Pockets
- 4 · best druggability 0.82
Structure
1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp synthase [glutamine-hydrolyzing] | protein | 525 | 35% helix, 26% strand | Q1I5K9 |
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 | 1153 | 0.82 | 0.83 | 95 | empty |
| 2 | 203 | 0.58 | 0.80 | 18 | empty |
| 3 | 63 | 0.49 | 0.85 | 17 | empty |
| 4 | 77 | 0.37 | 0.77 | 20 | 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 Q1I5K9
- Elsewhere: UniProt Q1I5K9 · AlphaFold DB Q1I5K9
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