Research workbench
AlphaFold monomer V2.0 prediction for serine carboxypeptidase-like 11 (Q2V465)
Analyse AlphaFold monomer V2.0 prediction for serine carboxypeptidase-like 11 (Q2V465) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2V465
- Type
- protein
- Length
- 433 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Serine carboxypeptidase-like 11
- UniProt
- Q2V465
- Pockets
- 6 · best druggability 0.58
Structure
1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine carboxypeptidase-like 11 | protein | 433 | 34% helix, 21% strand | Q2V465 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.58 | 0.80 | 34 | empty |
| 2 | 119 | 0.43 | 0.77 | 22 | empty |
| 3 | 86 | 0.38 | 0.76 | 27 | empty |
| 4 | 73 | 0.35 | 0.77 | 16 | empty |
| 5 | 58 | 0.29 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 4 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 Q2V465
- Elsewhere: UniProt Q2V465 · AlphaFold DB Q2V465
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