Crystallization (Comment) | Organism |
---|---|
component E1 without cofactors thiamine diphosphate and Mg2+, at 2.32 A resolution. Water molecules may form a hydrogen-bonded linkage between residues Glu571 and Val192, which normally make conserved interactions with the thiamine diphosphate cofactor. A histidine side chain that normally forms hydrogen bonds to thiamine diphosphate is disordered in its absence and partially occupies two sites. No disorder/order loop transformations are evident in the apo-E1 component relative to the holo-E1 enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AFG8 | E1 component AceE, cf. EC 1.2.4.1 | - |