MolNFT v1 · #250803 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A9AI95)
A9AI95: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A9AI95)”. 6 pockets (best druggability 0.61). MolNFT v1 #250803 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A9AI95
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A9AI95
- Pockets
- 6 · best druggability 0.61
Structure
1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 465 | 38% helix, 25% strand | A9AI95 |
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 | 207 | 0.61 | 0.82 | 32 | empty |
| 2 | 399 | 0.61 | 0.77 | 44 | empty |
| 3 | 69 | 0.35 | 0.77 | 14 | empty |
| 4 | 54 | 0.34 | 0.78 | 15 | empty |
| 5 | 65 | 0.32 | 0.75 | 17 | 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 A9AI95
- Elsewhere: UniProt A9AI95 · AlphaFold DB A9AI95
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