MolNFT v1 · #251210 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q12SC5)
Q12SC5: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q12SC5)”. 4 pockets (best druggability 0.75). MolNFT v1 #251210 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q12SC5
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q12SC5
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 479 | 38% helix, 25% strand | Q12SC5 |
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 | 1066 | 0.75 | 0.78 | 97 | empty |
| 2 | 51 | 0.35 | 0.79 | 15 | empty |
| 3 | 52 | 0.34 | 0.78 | 14 | empty |
| 4 | 51 | 0.30 | 0.76 | 13 | 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 Q12SC5
- Elsewhere: UniProt Q12SC5 · AlphaFold DB Q12SC5
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