EC Number   |
General Information |
Reference |
|---|
    1.15.1.2 | more |
iron reduction does not lead to dissociation of glutamate from the catalytic metal or other structural changes, but the glutamate ligand undergoes X-ray-induced chemical changes, revealing high sensitivity of the GiSOR active site to X-ray radiation damage, enzyme structure modeling and structure comparisons |
743942 |
| 1.15.1.2 | more |
key catalytic residue is E23, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112 |
-, 744687 |
| 1.15.1.2 | more |
key catalytic residue is K9, catalytic Fe2+ binding residues are H10, H35, H41, C97, and H100 |
744687 |
| 1.15.1.2 | more |
key catalytic residues are E12 and K13, catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113 |
744687 |
| 1.15.1.2 | more |
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114 |
-, 744687 |
| 1.15.1.2 | more |
key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118 |
-, 744687 |
| 1.15.1.2 | more |
key catalytic residues are E23, K24, H25, H50, H56, C111, and H114 |
744687 |
| 1.15.1.2 | more |
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118 |
-, 744687 |
| 1.15.1.2 | more |
key catalytic residues are E48, K40, H50, H70, H76, C119, and H122 |
-, 744687 |
| 1.15.1.2 | more |
model structure of SOR-rubredoxin complex, docking simulations, overview |
727313 |
