MolNFT v1 · #251628 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (B9EB51)
B9EB51 · Udp-N-acetylmuramoylalanine--D-glutamate ligase: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (B9EB51)”. 2 pockets (best druggability 0.71). MolNFT v1 #251628 on GenesisL1: 3D structure…
- Accession
- B9EB51
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd9e069D1339FAA95b9530BA8d5279541BF7Eeaab
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- B9EB51
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 445 | 36% helix, 21% strand | B9EB51 |
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 | 957 | 0.71 | 0.75 | 75 | empty |
| 2 | 136 | 0.43 | 0.75 | 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 B9EB51
- Elsewhere: UniProt B9EB51 · AlphaFold DB B9EB51
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