Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (C1F455)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1F455
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x10F20E5FD6223F71224Fba7496Eba14cf3dd37D0
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- C1F455
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 458 | 37% helix, 23% strand | C1F455 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.64 | 0.82 | 32 | empty |
| 2 | 369 | 0.60 | 0.77 | 34 | empty |
| 3 | 51 | 0.40 | 0.82 | 13 | empty |
| 4 | 60 | 0.38 | 0.80 | 12 | empty |
| 5 | 63 | 0.34 | 0.77 | 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 C1F455
- Elsewhere: UniProt C1F455 · AlphaFold DB C1F455
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