Reaction Details |
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Target | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
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Ligand | BDBM92264 |
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Substrate/Competitor | n/a |
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Meas. Tech. | Thermofluor |
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pH | 7±n/a |
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Temperature | 298.15±n/a K |
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Kd | >100000±n/a nM |
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Citation | CSARdock, CD LPXC in CSAR_FULL_RELEASE_3JULY2012 CSAR1:0 (2012) |
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More Info.: | Get all data from this article, Solution Info, Assay Method |
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UDP-3-O-acyl-N-acetylglucosamine deacetylase |
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Name: | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
Synonyms: | LPXC_AQUAE | UDP-3-O-Acyl-GlcNAc Deacetylase (LpxC) | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase | envA | lpxC | zinc deacetylase LpxC |
Type: | Hydrolase |
Mol. Mass.: | 32146.02 |
Organism: | Aquifex aeolicus |
Description: | The enzyme was stripped of all metal ions by dialysis against 1.0 mM EDTA in buffer at room temperature. The EDTA was then removed by extensive dialysis against EDTA-free buffer and the enzyme was reconstituted to a 1:1 Zn2+ to LpxC ratio by the addition of ZnSO4. |
Residue: | 282 |
Sequence: | MGLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHEFVVHTNHST
DLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDGSGWEFYEAIRKNILNQNRE
IDYFVVEEPIIVEDEGRLIKAEPSDTLEVTYEGEFKNFLGRQKFTFVEGNEEEIVLARTF
CFDWEIEHIKKVGLGKGGSLKNTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGS
PVKGKFYSFRGGHSLNVKLVKELAKKQKLTRDLPHLPSVQAL
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BDBM92264 |
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n/a |
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Name | BDBM92264 |
Synonyms: | CS254 |
Type | n/a |
Emp. Form. | C24H24N4O5 |
Mol. Mass. | 448.4712 |
SMILES | C[C@@H](O)[C@H](NC(=O)c1ccc(cc1)C#Cc1ccccc1)C(=O)NCC1(C)NC(=O)NC1=O |
Structure |
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