Research workbench
AlphaFold monomer V2.0 prediction for carbamoyl-phosphate synthase small chain (A5VRM1)
Analyse AlphaFold monomer V2.0 prediction for carbamoyl-phosphate synthase small chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VRM1
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9E72a6c28d20b2443a44F1c57457a027ddE4fa17
- Molecule
- Carbamoyl-phosphate synthase small chain
- UniProt
- A5VRM1
- Pockets
- 4 · best druggability 0.47
Structure
1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbamoyl-phosphate synthase small chain | protein | 407 | 24% helix, 31% strand | A5VRM1 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.47 | 0.75 | 32 | empty |
| 2 | 66 | 0.34 | 0.77 | 20 | empty |
| 3 | 58 | 0.33 | 0.77 | 14 | empty |
| 4 | 67 | 0.28 | 0.72 | 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 A5VRM1
- Elsewhere: UniProt A5VRM1 · AlphaFold DB A5VRM1
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