Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-L-alanyl- D-glutamate--2,6-diaminopimelate ligase (Q57TD5)
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
- Q57TD5
- Type
- protein
- Length
- 495 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7F0F83db3b9ec3a86cc0eDAaF6DE0950a3Ce107D
- Molecule
- Udp-N-acetylmuramoyl-L-alanyl-D-glutamate-- 2,6-diaminopimelate ligase
- UniProt
- Q57TD5
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoyl-L-alanyl-D-glutamate-- 2,6-diaminopimelate ligase | protein | 495 | 34% helix, 24% strand | Q57TD5 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.69 | 0.81 | 57 | empty |
| 2 | 156 | 0.61 | 0.84 | 29 | empty |
| 3 | 295 | 0.52 | 0.74 | 34 | 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 Q57TD5
- Elsewhere: UniProt Q57TD5 · AlphaFold DB Q57TD5
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