MolNFT v1 · #251611 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q5X1S4)
Q5X1S4 · Udp-N-acetylmuramoylalanine--D-glutamate ligase: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q5X1S4)”. 3 pockets (best druggability 0.68). MolNFT v1 #251611 on GenesisL1: 3D structure…
- Accession
- Q5X1S4
- Type
- protein
- Length
- 447 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0875F73396B4A0E8f4BD76671AdbDc2786B3f8B7
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q5X1S4
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 447 | 36% helix, 23% strand | Q5X1S4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 633 | 0.68 | 0.77 | 54 | empty |
| 2 | 406 | 0.65 | 0.79 | 62 | empty |
| 3 | 63 | 0.36 | 0.78 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q5X1S4
- Elsewhere: UniProt Q5X1S4 · AlphaFold DB Q5X1S4
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