Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-L-alanyl- D-glutamate--2,6-diaminopimelate ligase (Q87AF5)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-L-alanyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q87AF5
- Type
- protein
- Length
- 495 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf210F5B89b6A859c8E395243D7942e4739F3DC69
- Molecule
- Udp-N-acetylmuramoyl-L-alanyl-D-glutamate-- 2,6-diaminopimelate ligase
- UniProt
- Q87AF5
- Pockets
- 2 · best druggability 0.74
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoyl-L-alanyl-D-glutamate-- 2,6-diaminopimelate ligase | protein | 495 | 36% helix, 23% strand | Q87AF5 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 668 | 0.74 | 0.81 | 86 | empty |
| 2 | 319 | 0.59 | 0.77 | 43 | 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 Q87AF5
- Elsewhere: UniProt Q87AF5 · AlphaFold DB Q87AF5
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