MolNFT v1 · #250716 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5E2Q1)
Q5E2Q1: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5E2Q1)”. 2 pockets (best druggability 0.76). MolNFT v1 #250716 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5E2Q1
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35cE46a4a30196447966Bd34E1e090Eb6D1bAd3f
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q5E2Q1
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 487 | 39% helix, 24% strand | Q5E2Q1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.76 | 0.79 | 92 | empty |
| 2 | 62 | 0.33 | 0.76 | 12 | 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 Q5E2Q1
- Elsewhere: UniProt Q5E2Q1 · AlphaFold DB Q5E2Q1
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