EC Number   |
Reference |
|---|
   3.4.24.36 | homology modeling based on the structure of Leishmania major gp63. The protein consists of the N-terminal, central and C-terminal domain |
696516 |
| 3.4.24.36 | Leishmania major, crystallographic parameters |
31228 |
| 3.4.24.36 | molecular dynamics simulation of enzyme in water. Upon solvation, enzyme undergoes a sharp structural relaxation with respect to the crystal structure. Fingerprint fluctuations of enzyme are characterized by the motion of a large part of the N-terminal domain, which is also involved in substrate recognition and proenzyme activation. Residues involved in interdomain binding are highly conserved |
670848 |
| 3.4.24.36 | monoclinic crystals, space group C2 with a : 107.2 A, b : 90.6 A, c : 70.6 A, and tetragonal crystals, space group P4(1)2(1)2(1), a : b : 63.6 A, c : 251.4 A |
653919 |
