Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (P17443)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P17443
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD0Df07413FbF205CF8f5e551F4Bc6E7250CE2998
- Molecule
- Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol…
- UniProt
- P17443
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase | protein | 355 | 47% helix, 15% strand | P17443 |
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 | 748 | 0.69 | 0.76 | 76 | empty |
| 2 | 59 | 0.50 | 0.86 | 18 | empty |
Compared structures
- 1NLM · Crystal structure of MURG:GLCNAC complex · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 1NLM · Crystal structure of MURG:GLCNAC complex · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 1F0K · The 1.9 ångström crystal structure of E. COLI murg · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 1F0K · The 1.9 ångström crystal structure of E. COLI murg · an experimental structure of the same protein · chain A against A, TM-score 0.93
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 P17443
- Elsewhere: UniProt P17443 · AlphaFold DB P17443
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