MolNFT v1 · #250704 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B5ELC2)
B5ELC2: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B5ELC2)”. 3 pockets (best druggability 0.65). MolNFT v1 #250704 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- B5ELC2
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B5ELC2
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 464 | 36% helix, 26% strand | B5ELC2 |
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 | 211 | 0.65 | 0.84 | 30 | empty |
| 2 | 427 | 0.63 | 0.78 | 48 | empty |
| 3 | 59 | 0.31 | 0.76 | 14 | 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 B5ELC2
- Elsewhere: UniProt B5ELC2 · AlphaFold DB B5ELC2
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