EC Number   |
|---|
  2.3.1.301 | enzyme in complex with inhibitor CoA methyldisulfide |
| 2.3.1.301 | structure of mutant C112A with lauroyl-coenzyme A. An elongated channelextending from the mutated active-site cysteine defines the acyl group binding locus. CoA lies in a second channel, bound primarily through interactions of its nucleotide group at the enzyme surface |
| 2.3.1.301 | strucure of FabH with CoAdecyl disulfide inhibitor. The decyl chain binds in acyl-binding channels of both subunits through disulfide linkage to the active site cysteine. Both subunits of FabH can react with substrates or inhibitor |
| 2.3.1.301 | strucure to 2.1 A resolution. A CoA/malonyl-ACP-binding channel leads from the enzyme surface to the buried active-site cysteine residue, and a second hydrophobic channel leads from the active site. In the ecFabH structure, this channel is blocked by a phenylalanine residue, whereas in Microbacterium tuberculosisFabH, this residue is a threonine, which permits binding of longer acyl chains |
| 2.3.1.301 | wild-type and mutant A246F in complex with inhibitors |
