Crystallization (Comment) | Organism |
---|---|
to 2.1 A resolution. LOX crystallizes as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. Residues Tyr40, Arg268, His265, Tyr146 and Asp174 are involved in substrate binding | Aerococcus viridans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aerococcus viridans | Q44467 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
LOX | - |
Aerococcus viridans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | FMN is positioned deep down in the funnel-shaped substrate-binding site, behind (or underneath) the substrate when it is bound. Residues Tyr40, Pro93, Gln144, Tyr146, Thr172, Lys241, Asp296, Arg300 and Arg320 are involved in binding | Aerococcus viridans |