Research workbench
AlphaFold monomer V2.0 prediction for endolytic peptidoglycan transglycosylase rlpa (Q9PHM1)
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
- Q9PHM1
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Endolytic peptidoglycan transglycosylase rlpa
- UniProt
- Q9PHM1
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 10% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolytic peptidoglycan transglycosylase rlpa | protein | 275 | 10% helix, 29% strand | Q9PHM1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.69 | 0.88 | 30 | empty |
| 2 | 61 | 0.30 | 0.75 | 16 | 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 Q9PHM1
- Elsewhere: UniProt Q9PHM1 · AlphaFold DB Q9PHM1
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