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Literature summary for 2.3.1.129 extracted from
- LpxA: a natural nanotube (2010), Biopolymers, 93, 845-853.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotrimer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LpxA | - |
Escherichia coli |
| UDP-N-acetylglucosamine 3-O-acyltransferase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | UDP-N-acetylglucosamine 3-O-acyltransferase is a protein with a left-handed parallel beta-helix, which is a natural nanotube associated with unusual high stability, molecular dynamics simulations using LpxA crystal structure, PDB ID 1LXA, and formation of a dynamical cross-correlation map, overview. Construction of the unfolding conformational energy landscape identifies the probable intermediates that can appear in the unfolding pathway of the protein, unfolding kinetics of the three-stranded beta-sheet protein, overview | Escherichia coli |
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Release 2023.1 (January 2023)
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