Crystallization (Comment) | Organism |
---|---|
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe) | Mus musculus |
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe). The mAOX1 isoform has the wider specificity region with a variety of polar and charged amino acids | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q148T8 | - |
- |
Mus musculus | Q5SGK3 | - |
- |
Mus musculus | Q8R387 | - |
- |
Mus musculus | Q8VI15 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AOX1 | - |
Mus musculus |
AOX2 | - |
Mus musculus |