MolNFT v1 · #250981 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5R0M0)
Q5R0M0: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5R0M0)”. 3 pockets (best druggability 0.74). MolNFT v1 #250981 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5R0M0
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x13D0a95FDcd918ebb5150FD2C57cfC72eC29DA05
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q5R0M0
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 490 | 35% helix, 25% strand | Q5R0M0 |
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 | 832 | 0.74 | 0.79 | 79 | empty |
| 2 | 73 | 0.37 | 0.77 | 16 | empty |
| 3 | 53 | 0.34 | 0.79 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q5R0M0
- Elsewhere: UniProt Q5R0M0 · AlphaFold DB Q5R0M0
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