MolNFT v1 · #251603 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q9CF91)
Q9CF91 · Udp-N-acetylmuramoylalanine--D-glutamate ligase: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q9CF91)”. 2 pockets (best druggability 0.69). MolNFT v1 #251603 on GenesisL1: 3D structure…
- Accession
- Q9CF91
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x904d84aaC5C1E7049458cDf50F391bfC907AF1cA
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q9CF91
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 450 | 39% helix, 21% strand | Q9CF91 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.69 | 0.75 | 81 | empty |
| 2 | 95 | 0.40 | 0.76 | 18 | 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 Q9CF91
- Elsewhere: UniProt Q9CF91 · AlphaFold DB Q9CF91
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