Research workbench
AlphaFold monomer V2.0 prediction for putative serine protease K12H4.7 (P34528)
Analyse AlphaFold monomer V2.0 prediction for putative serine protease K12H4.7 (P34528) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P34528
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Putative serine protease K12H4.7
- UniProt
- P34528
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative serine protease K12H4.7 | protein | 510 | 49% helix, 14% strand | P34528 |
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 | 123 | 0.41 | 0.75 | 20 | empty |
| 2 | 95 | 0.37 | 0.76 | 20 | empty |
| 3 | 70 | 0.33 | 0.76 | 17 | empty |
| 4 | 60 | 0.32 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 3 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 P34528
- Elsewhere: UniProt P34528 · AlphaFold DB P34528
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