Research workbench
AlphaFold monomer V2.0 prediction for peptidoglycan endopeptidase ripa (A0QX22)
Analyse AlphaFold monomer V2.0 prediction for peptidoglycan endopeptidase ripa (A0QX22) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0QX22
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Peptidoglycan endopeptidase ripa
- UniProt
- A0QX22
- Pockets
- 2 · best druggability 0.64
Structure
1 distinct chain · 52% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan endopeptidase ripa | protein | 497 | 52% helix, 8% strand | A0QX22 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.64 | 0.92 | 25 | empty |
| 2 | 311 | 0.54 | 0.75 | 33 | empty |
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 A0QX22
- Elsewhere: UniProt A0QX22 · AlphaFold DB A0QX22
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