Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B9MND8)
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
- B9MND8
- Type
- protein
- Length
- 455 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c860Cd4B4aF5cd0B224EEce054f91b534Db0285
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B9MND8
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 455 | 37% helix, 26% strand | B9MND8 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 762 | 0.72 | 0.78 | 66 | empty |
| 2 | 262 | 0.64 | 0.82 | 42 | 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 B9MND8
- Elsewhere: UniProt B9MND8 · AlphaFold DB B9MND8
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