Research workbench
AlphaFold monomer V2.0 prediction for peptidoglycan D,D-transpeptidase mrda (P0CL14)
Analyse AlphaFold monomer V2.0 prediction for peptidoglycan D,D-transpeptidase mrda… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CL14
- Type
- protein
- Length
- 623 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDf921891Aa1d2eaE579c7ab7a9c178c8fb3840ec
- Molecule
- Peptidoglycan D,D-transpeptidase mrda
- UniProt
- P0CL14
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan D,D-transpeptidase mrda | protein | 623 | 41% helix, 21% strand | P0CL14 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.66 | 0.77 | 52 | empty |
| 2 | 509 | 0.62 | 0.75 | 51 | empty |
| 3 | 62 | 0.31 | 0.75 | 14 | empty |
| 4 | 53 | 0.25 | 0.73 | 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 P0CL14
- Elsewhere: UniProt P0CL14 · AlphaFold DB P0CL14
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