MolNFT v1 · #250901 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A1VBE9)
A1VBE9: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A1VBE9)”. 3 pockets (best druggability 0.66). MolNFT v1 #250901 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A1VBE9
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3048035c88f5559a84b15475ED6c0013b3E8bF25
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A1VBE9
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 454 | 36% helix, 25% strand | A1VBE9 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 502 | 0.66 | 0.78 | 55 | empty |
| 2 | 211 | 0.60 | 0.81 | 31 | empty |
| 3 | 58 | 0.30 | 0.75 | 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 A1VBE9
- Elsewhere: UniProt A1VBE9 · AlphaFold DB A1VBE9
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