Structure of Leishmania major peroxidase D211R mutant (high res)

Enzymatic Mechanism of Leishmania major Peroxidase and the Critical Role of Specific Ionic Interactions.

C-TERMINAL CATALYTIC DOMAIN, RESIDUES 35-303

SEEPPFDIRALRADIEDMISEKLELGPSLIRLAWHEAASYDCFKKDGSPNSASMRFKPECLYAGNKGLDIPRKALETLKK
KYPQISYADLWVLAAYVAIEYMGGPTIPFCWGRVDAKDGSVCGPDGRLPDGSKTQSHVREVFRRLGFNDQETVALIGAHT
CGECHIEFSGYHGPWTHRKNGFDNSFFTQLLDEDWVLNPKVEQMQLMDRATTKLMMLPSDVCLLLDPSYRKYVELYAKDN
DRFNKDFANAFKKLTELGTRNLHKAPASES

10% PEG MME 5000, 0.1M MES:NAOH PH 6.5, 5% DMSO, 7.5 MM PRASEODIMIUM(III) ACETATE HYDRATE

STRUCTURE OF LEISHMANIA MAJOR PEROXIDASE D211R MUTANT ( LOW RES)

PROTOPORPHYRIN IX CONTAINING FE (HEM): THERE IS A POSITIVE DENSITY CONSISTENT WITH A DIATOMIC MOLECULE COVALENTLY LINKED TO THE HEME MESO- CARBON CHB