Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-tripeptide --D-alanyl-D-alanine ligase (Q92H60)
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
- Q92H60
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7F03E9F55aBE36b392B9aDB35ac1C267e9A2BC53
- Molecule
- Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UniProt
- Q92H60
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase | protein | 449 | 38% helix, 23% strand | Q92H60 |
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 | 573 | 0.74 | 0.82 | 71 | empty |
| 2 | 59 | 0.33 | 0.77 | 14 | empty |
| 3 | 64 | 0.33 | 0.76 | 23 | empty |
| 4 | 55 | 0.24 | 0.72 | 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 Q92H60
- Elsewhere: UniProt Q92H60 · AlphaFold DB Q92H60
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