MolNFT v1 · #250388 · protein
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (A5FNG4)
A5FNG4 · Udp-N-acetylenolpyruvoylglucosamine reductase: “AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (A5FNG4)”. 2 pockets (best druggability 0.81). MolNFT v1 #250388 on GenesisL1: 3D structure…
- Accession
- A5FNG4
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- A5FNG4
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 337 | 27% helix, 28% strand | A5FNG4 |
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 | 1110 | 0.81 | 0.82 | 98 | empty |
| 2 | 71 | 0.34 | 0.76 | 17 | 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 A5FNG4
- Elsewhere: UniProt A5FNG4 · AlphaFold DB A5FNG4
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