Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (Q5XC20)
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
- Q5XC20
- Type
- protein
- Length
- 520 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc87019A1CC09AD435548CEeAeAc61B1e4Ca83541
- Molecule
- Gmp synthase [glutamine-hydrolyzing]
- UniProt
- Q5XC20
- Pockets
- 7 · best druggability 0.72
Structure
1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp synthase [glutamine-hydrolyzing] | protein | 520 | 35% helix, 24% strand | Q5XC20 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.72 | 0.80 | 62 | empty |
| 2 | 106 | 0.42 | 0.77 | 21 | empty |
| 3 | 107 | 0.42 | 0.77 | 19 | empty |
| 4 | 66 | 0.32 | 0.76 | 19 | empty |
| 5 | 52 | 0.32 | 0.77 | 12 | 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 Q5XC20
- Elsewhere: UniProt Q5XC20 · AlphaFold DB Q5XC20
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