MolNFT v1 · #250727 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B4UES2)
B4UES2: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B4UES2)”. 3 pockets (best druggability 0.72). MolNFT v1 #250727 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- B4UES2
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B4UES2
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 458 | 38% helix, 25% strand | B4UES2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 712 | 0.72 | 0.79 | 75 | empty |
| 2 | 55 | 0.33 | 0.77 | 12 | empty |
| 3 | 76 | 0.32 | 0.74 | 12 | 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 B4UES2
- Elsewhere: UniProt B4UES2 · AlphaFold DB B4UES2
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