EC Number   |
Reference  |
|---|
    1.20.4.1 | comparative homology modeling. Along with Cys11, the residues like Ile8, Pro9, Asn10, Gly12, Thr13, Cys14, Lys15, and Phe18 also show coordination with arsenate |
727580 |
| 1.20.4.1 | in silico modeling of disulfide bonds into the solution NMR structure of the fully-reduced enzyme. C8/C82 and C80C82 disulfides are equally consistent |
727076 |
| 1.20.4.1 | molecular modeing of structure. Residues Cys12, Arg60, Arg94, and Arg107 are identified as metal binding residues |
728218 |
| 1.20.4.1 | molecular modeling and docking with asenate oxyanion. Residues Cys11, Ile8, Pro9, Asn10, Gly12, Thr13, Cys14, Lys15, and Phe18 show coordination with arsenate |
727580 |
