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AlphaFold monomer V2.0 prediction for palmitoleoyl-protein carboxylesterase NOTUM1A (C5H5C4)
Analyse AlphaFold monomer V2.0 prediction for palmitoleoyl-protein carboxylesterase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5H5C4
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xca0994581703679AaE6614F91C3dB368c35c7353
- Molecule
- Palmitoleoyl-protein carboxylesterase NOTUM1A
- UniProt
- C5H5C4
- Pockets
- 4 · best druggability 0.51
Structure
1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Palmitoleoyl-protein carboxylesterase NOTUM1A | protein | 500 | 38% helix, 14% strand | C5H5C4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.51 | 0.80 | 23 | empty |
| 2 | 81 | 0.44 | 0.80 | 15 | empty |
| 3 | 83 | 0.37 | 0.76 | 12 | empty |
| 4 | 67 | 0.33 | 0.76 | 20 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
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 C5H5C4
- Elsewhere: UniProt C5H5C4 · AlphaFold DB C5H5C4
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