Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q4FQW0)
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
- Q4FQW0
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7AaBC15ca535FA309169502EE67F5d02D4116236
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q4FQW0
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 479 | 34% helix, 24% strand | Q4FQW0 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.76 | 0.78 | 94 | empty |
| 2 | 79 | 0.43 | 0.80 | 21 | empty |
| 3 | 116 | 0.40 | 0.75 | 16 | empty |
| 4 | 66 | 0.35 | 0.78 | 16 | empty |
| 5 | 57 | 0.29 | 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 Q4FQW0
- Elsewhere: UniProt Q4FQW0 · AlphaFold DB Q4FQW0
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