Research workbench
AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein 3 (Q765P2)
Analyse AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q765P2
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Peptidoglycan-recognition protein 3
- UniProt
- Q765P2
- Pockets
- 2 · best druggability 0.42
Structure
1 distinct chain · 24% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan-recognition protein 3 | protein | 187 | 24% helix, 18% strand | Q765P2 |
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 | 94 | 0.42 | 0.78 | 23 | empty |
| 2 | 54 | 0.30 | 0.75 | 12 | 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 Q765P2
- Elsewhere: UniProt Q765P2 · AlphaFold DB Q765P2
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