Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-tripeptide --D-alanyl-D-alanine ligase (P96613)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-tripeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P96613
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UniProt
- P96613
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase | protein | 457 | 38% helix, 22% strand | P96613 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.70 | 0.80 | 55 | empty |
| 2 | 83 | 0.43 | 0.79 | 19 | empty |
| 3 | 106 | 0.37 | 0.74 | 18 | empty |
| 4 | 53 | 0.28 | 0.74 | 15 | 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 P96613
- Elsewhere: UniProt P96613 · AlphaFold DB P96613
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