MolNFT v1 · #250874 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B1VHC3)
B1VHC3: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B1VHC3)”. 4 pockets (best druggability 0.73). MolNFT v1 #250874 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- B1VHC3
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B1VHC3
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 487 | 37% helix, 24% strand | B1VHC3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 803 | 0.73 | 0.78 | 86 | empty |
| 2 | 114 | 0.39 | 0.75 | 23 | empty |
| 3 | 61 | 0.31 | 0.75 | 18 | empty |
| 4 | 56 | 0.30 | 0.76 | 20 | 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 B1VHC3
- Elsewhere: UniProt B1VHC3 · AlphaFold DB B1VHC3
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