MolNFT v1 · #428584 · protein
AlphaFold monomer V2.0 prediction for cmp-N-acetylneuraminate-poly- alpha-2,8-sialyltransferase (Q92187)
Q92187 · Cmp-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase: “AlphaFold monomer V2.0 prediction for cmp-N-acetylneuraminate-poly- alpha-2,8-sialyltransferase (Q92187)”. 5 pockets (best druggability 0.74). MolNFT v1 #428584 on…
- Accession
- Q92187
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x69eE01C8f0EE6680BfD1adfA715C501Aba23F4B9
- Molecule
- Cmp-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase
- UniProt
- Q92187
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cmp-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase | protein | 359 | 44% helix, 13% strand | Q92187 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.74 | 0.86 | 43 | empty |
| 2 | 477 | 0.66 | 0.78 | 45 | empty |
| 3 | 66 | 0.41 | 0.81 | 16 | empty |
| 4 | 99 | 0.36 | 0.75 | 22 | empty |
| 5 | 77 | 0.33 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6AHZ · The NMR structure of the polysialyltranseferase domain (pstd) in polysialyltransferase… · an experimental structure of the same protein · chain A against A, TM-score 0.07
- 5Y3U · NMR-based model of the 22 amino acid peptide in polysialyltransferase domain (pstd) of… · an experimental structure of the same protein · chain A against A, TM-score 0.05
- 5Y22 · NMR-based model of the 22 amino acid peptide in polysialyltransferase domain (pstd) of… · an experimental structure of the same protein · chain A against A, TM-score 0.05
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 Q92187
- Elsewhere: UniProt Q92187 · AlphaFold DB Q92187
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