Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (A5FHB4)
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
- A5FHB4
- Type
- protein
- Length
- 509 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5B92Ca2886C109632BF8623f55418EAeaf0DD1AD
- Molecule
- Gmp synthase [glutamine-hydrolyzing]
- UniProt
- A5FHB4
- Pockets
- 5 · best druggability 0.82
Structure
1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp synthase [glutamine-hydrolyzing] | protein | 509 | 32% helix, 26% strand | A5FHB4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1178 | 0.82 | 0.83 | 100 | empty |
| 2 | 117 | 0.49 | 0.80 | 18 | empty |
| 3 | 88 | 0.44 | 0.80 | 18 | empty |
| 4 | 69 | 0.39 | 0.79 | 18 | empty |
| 5 | 54 | 0.30 | 0.75 | 15 | 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 A5FHB4
- Elsewhere: UniProt A5FHB4 · AlphaFold DB A5FHB4
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