EC Number   |
Subunits |
Reference |
|---|
   2.7.1.171 | ? |
x * 35000, calculated from sequence |
708295 |
| 2.7.1.171 | ? |
x * 35000, SDS-PAGE |
707420, 708294 |
| 2.7.1.171 | ? |
x * 35032, calculated from sequence |
707061, 708294 |
| 2.7.1.171 | ? |
x * 35171, calculated from sequence |
708294 |
| 2.7.1.171 | dimer |
- |
762465 |
| 2.7.1.171 | dimer |
the crystal structure of the FN3K homologue from Arabidopsis thaliana reveals that it forms an unexpected strand-exchange dimer in which the ATP-binding P-loop and adjoining beta-strands are swapped between two chains in the dimer. This dimeric configuration is characterized by strained interchain disulfide bonds that stabilize the P-loop in an extended conformation. In the AtFN3K dimer, the substrate-binding lobes are covalently tethered to create a unique interface, presumably for phosphorylating ketosamine and related substrates. AtFN3K can dimerize without the cysteines |
762465 |
| 2.7.1.171 | monomer |
- |
762465 |
| 2.7.1.171 | More |
FN3K adopts a protein kinase fold. Structure-function analysis and comparisons, overview |
762465 |
| 2.7.1.171 | More |
FN3K adopts a protein kinase fold. The wild-type and mutant enzymes show both dimeric and monomeric forms, structure-function analysis and comparisons, overview |
762465 |
