Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (Q13XE2)
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
- Q13XE2
- Type
- protein
- Length
- 527 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6422D1F59417BB8FF3023d32BEd5e42a2DAda950
- Molecule
- Gmp synthase [glutamine-hydrolyzing]
- UniProt
- Q13XE2
- Pockets
- 6 · best druggability 0.79
Structure
1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp synthase [glutamine-hydrolyzing] | protein | 527 | 35% helix, 26% strand | Q13XE2 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.79 | 0.80 | 71 | empty |
| 2 | 167 | 0.55 | 0.80 | 18 | empty |
| 3 | 207 | 0.50 | 0.76 | 26 | empty |
| 4 | 137 | 0.47 | 0.78 | 28 | empty |
| 5 | 95 | 0.43 | 0.78 | 21 | 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 Q13XE2
- Elsewhere: UniProt Q13XE2 · AlphaFold DB Q13XE2
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