Crystallization (Comment) | Organism |
---|---|
apo-enzyme, to 1.39 A resolution, and in complex with NADP+. Enzyme accepts both cofactors NADH and NADPH. Insertions near the N-terminus of the specificity loop probably determine cofactor specificity, the laboratory engineering of NADH preference involved specific loop substitution | Ignisphaera aggregans |
in complex with NADH, to 1.54 A resolution. The specificity loop differs significantly from any other crystallized ketol-acid reductoisomerases. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2' hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55 | uncultured archaeon |
in complex with substrate analog L-tartaric acid, to 2.5 A resolution. The enzyme displays a six-member specificity loop, with residues Arg48 and Ser52 forming hydrogen bonds to the NAD(H) phosphate | Alicyclobacillus acidocaldarius subsp. acidocaldarius |
to 1.54 A resolution. Structure contains 2 Mg2+ ions and NADH. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2 hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55 | uncultured archaeon GZfos26G2 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alicyclobacillus acidocaldarius subsp. acidocaldarius | C8WR67 | cf. EC 1.1.1.86 | - |
Ignisphaera aggregans | E0SRA9 | - |
- |
Ignisphaera aggregans DSM 17230 | E0SRA9 | - |
- |
uncultured archaeon | Q64BR7 | cf. 1.1.1.86 | - |
uncultured archaeon GZfos26G2 | Q64BR7 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
ilvC | - |
uncultured archaeon GZfos26G2 |
ilvC | - |
Ignisphaera aggregans |
ilvC | - |
Alicyclobacillus acidocaldarius subsp. acidocaldarius |
ilvC | - |
uncultured archaeon |