Research workbench
AlphaFold monomer V2.0 prediction for pirin-like protein yhak (P42624)
Analyse AlphaFold monomer V2.0 prediction for pirin-like protein yhak (P42624) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P42624
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Pirin-like protein yhak
- UniProt
- P42624
- Pockets
- 1 · best druggability 0.46
Structure
1 distinct chain · 1% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pirin-like protein yhak | protein | 233 | 1% helix, 56% strand | P42624 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.46 | 0.80 | 24 | empty |
Compared structures
- 2VEC · The crystal structure of the protein YhaK from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 2VEC · The crystal structure of the protein yhak from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.86
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 P42624
- Elsewhere: UniProt P42624 · AlphaFold DB P42624
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