CARBOXYLIC ESTER HYDROLASE, 1.5 ANGSTROM ORTHORHOMBIC FORM OF THE BOVINE RECOMBINANT PLA2
High-resolution refinement of orthorhombic bovine pancreatic phospholipase A2.
Crystal Structure of the Complex of Bovine Pancreatic Phospholipase A2 with a Transition State Analogue
1.72A Resolution Refinement of the Trigonal Form of Bovine Pancreatic Phospholipase A2
Crystal Structure of the Complex of Bovine Pancreatic Phospholipase A2 with the Inhibitor 1-Hexadecyl-3-(Trifluoroethyl)-Sn-Glycero-2-Phosphomethanol
Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-99
Phospholipase A2 Engineering. Deletion of the C-Terminus Segment Changes Substrate Specificity and Uncouples Calcium and Substrate Binding at the Zwitterionic Interface
Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence for the Interaction of Lysine-56 with Substrates
ALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNN EITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC
CRYSTALS WERE GROWN BY CO-CRYSTALLIZATION BY THE HANGING DROP VAPOR DIFFUSION METHOD USING THE CONDITIONS 5 (MICRO)L OF THE PROTEIN (15 MG/ML OF THE PROTEIN), 5MM CACL2, 50MM TRIS BUFFER, PH 7.2 AND 3.0 (MICRO)L OF 50% MPD IN THE DROPLET. THE RESERVOIR CONTAINED (50%) OF MPD., vapor diffusion - hanging drop
THE HIGH RESOLUTION ATOMIC COORDINATES OF THE WILD TYPE (PDB ENTRY 1BP2) WERE USED AS THE STARTING MODEL FOR REFINEMENT.
HYDROLASE, ENZYME, CARBOXYLIC ESTER HYDROLASE
MRLLVLAALLTVGAGQAGLNSRALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKL DSCKVLVDNPYTNNYSYSCSNNEITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC