Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (B9JY52)
Analyse AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9JY52
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x676cea925913029B25bFd75c68A60e44291ADf58
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- B9JY52
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 324 | 31% helix, 27% strand | B9JY52 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.77 | 0.84 | 61 | empty |
| 2 | 141 | 0.45 | 0.76 | 24 | empty |
| 3 | 63 | 0.31 | 0.75 | 14 | 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 B9JY52
- Elsewhere: UniProt B9JY52 · AlphaFold DB B9JY52
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