Research workbench
AlphaFold monomer V2.0 prediction for endolytic peptidoglycan transglycosylase rlpa (Q9K1A0)
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
- Q9K1A0
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x655E68DE706FB688fD0caB2F52eEf807C7bc553a
- Molecule
- Endolytic peptidoglycan transglycosylase rlpa
- UniProt
- Q9K1A0
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 18% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolytic peptidoglycan transglycosylase rlpa | protein | 239 | 18% helix, 30% strand | Q9K1A0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.44 | 0.83 | 12 | empty |
| 2 | 96 | 0.33 | 0.73 | 18 | empty |
| 3 | 58 | 0.31 | 0.76 | 18 | 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 Q9K1A0
- Elsewhere: UniProt Q9K1A0 · AlphaFold DB Q9K1A0
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