MolNFT v1 · #251315 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (C5BP33)
C5BP33: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (C5BP33)”. 5 pockets (best druggability 0.75). MolNFT v1 #251315 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- C5BP33
- Type
- protein
- Length
- 473 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- C5BP33
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 473 | 37% helix, 25% strand | C5BP33 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.75 | 0.79 | 81 | empty |
| 2 | 56 | 0.38 | 0.80 | 19 | empty |
| 3 | 61 | 0.33 | 0.77 | 14 | empty |
| 4 | 68 | 0.32 | 0.75 | 15 | empty |
| 5 | 57 | 0.28 | 0.74 | 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 C5BP33
- Elsewhere: UniProt C5BP33 · AlphaFold DB C5BP33
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