Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q4FPK6)
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
- Q4FPK6
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x126FAC61adfcCB9Aa6cE867C9C038cCe03399896
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q4FPK6
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 464 | 34% helix, 25% strand | Q4FPK6 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 827 | 0.74 | 0.78 | 79 | empty |
| 2 | 194 | 0.67 | 0.86 | 29 | empty |
| 3 | 71 | 0.43 | 0.81 | 19 | empty |
| 4 | 112 | 0.40 | 0.75 | 28 | empty |
| 5 | 85 | 0.35 | 0.75 | 17 | 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 Q4FPK6
- Elsewhere: UniProt Q4FPK6 · AlphaFold DB Q4FPK6
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