Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B1WQL2)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1WQL2
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2bC32f18fAE37A281d59d6b3aF4271fbb7011463
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B1WQL2
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 518 | 39% helix, 22% strand | B1WQL2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 856 | 0.74 | 0.79 | 67 | empty |
| 2 | 202 | 0.62 | 0.83 | 31 | empty |
| 3 | 91 | 0.36 | 0.75 | 21 | empty |
| 4 | 93 | 0.35 | 0.74 | 19 | 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 B1WQL2
- Elsewhere: UniProt B1WQL2 · AlphaFold DB B1WQL2
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