Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (C5BP36)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5BP36
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3048035c88f5559a84b15475ED6c0013b3E8bF25
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- C5BP36
- Pockets
- 5 · best druggability 0.55
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 453 | 36% helix, 23% strand | C5BP36 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.55 | 0.76 | 36 | empty |
| 2 | 96 | 0.37 | 0.75 | 20 | empty |
| 3 | 64 | 0.31 | 0.75 | 14 | empty |
| 4 | 64 | 0.28 | 0.73 | 24 | empty |
| 5 | 53 | 0.28 | 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 C5BP36
- Elsewhere: UniProt C5BP36 · AlphaFold DB C5BP36
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