Research workbench
AlphaFold monomer V2.0 prediction for endolytic peptidoglycan transglycosylase rlpa (Q9X6V6)
Analyse AlphaFold monomer V2.0 prediction for endolytic peptidoglycan transglycosylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9X6V6
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Endolytic peptidoglycan transglycosylase rlpa
- UniProt
- Q9X6V6
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 13% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolytic peptidoglycan transglycosylase rlpa | protein | 342 | 13% helix, 23% strand | Q9X6V6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.58 | 0.78 | 45 | empty |
| 2 | 153 | 0.49 | 0.78 | 22 | empty |
| 3 | 219 | 0.48 | 0.75 | 26 | 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 Q9X6V6
- Elsewhere: UniProt Q9X6V6 · AlphaFold DB Q9X6V6
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