Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (Q7VEH5)
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
- Q7VEH5
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x77ff9F5FE96bfF71D9917d1E205819107Ca1f53E
- Molecule
- Gmp synthase [glutamine-hydrolyzing]
- UniProt
- Q7VEH5
- Pockets
- 6 · best druggability 0.79
Structure
1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp synthase [glutamine-hydrolyzing] | protein | 528 | 34% helix, 22% strand | Q7VEH5 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.79 | 0.81 | 83 | empty |
| 2 | 169 | 0.57 | 0.81 | 18 | empty |
| 3 | 114 | 0.39 | 0.75 | 22 | empty |
| 4 | 100 | 0.37 | 0.75 | 15 | empty |
| 5 | 102 | 0.34 | 0.73 | 24 | 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 Q7VEH5
- Elsewhere: UniProt Q7VEH5 · AlphaFold DB Q7VEH5
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