Research workbench
AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein 1 (Q765P4)
Analyse AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q765P4
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb92D3b0E198eC4a6c8dCd4D0aFDD2FC07B271c2C
- Molecule
- Peptidoglycan-recognition protein 1
- UniProt
- Q765P4
- Pockets
- 2 · best druggability 0.33
Structure
1 distinct chain · 30% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan-recognition protein 1 | protein | 197 | 30% helix, 17% strand | Q765P4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.33 | 0.76 | 11 | empty |
| 2 | 75 | 0.33 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 2 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 Q765P4
- Elsewhere: UniProt Q765P4 · AlphaFold DB Q765P4
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