1KVY

CARBOXYLIC ESTER HYDROLASE, SINGLE MUTANT D49E COORDINATED TO CALCIUM

Summary for 1KVY

• Entry DOI: 10.2210/pdb1kvy/pdb
• Descriptor: PHOSPHOLIPASE A2, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase, enzyme, carboxylic ester hydrolase, mutant
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00593
• Total number of polymer chains: 1
• Total formula weight: 13864.61

Authors

Sundaralingam, M. (deposition date: 1998-04-29, release date: 1998-11-18, Last modification date: 2024-10-23)

Primary citation

Sekar, K.,Biswas, R.,Li, Y.,Tsai, M.,Sundaralingam, M.
Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.
Acta Crystallogr.,Sect.D, 55:443-447, 1999

PubMed Abstract: Crystal structures of the active-site mutants D99A and H48Q and the calcium-loop mutant D49E of bovine phospholipase A2 have been determined at around 1.9 A resolution. The D99A mutant is isomorphous to the orthorhombic recombinant enzyme, space group P212121. The H48Q and the calcium-loop mutant D49E are isomorphous to the trigonal recombinant enzyme, space group P3121. The two active-site mutants show no major structural perturbations. The structural water is absent in D99A and, therefore, the hydrogen-bonding scheme is changed. In H48Q, the catalytic water is present and hydrogen bonded to Gln48 N, but the second water found in native His48 is absent. In the calcium-loop mutant D49E, the two water molecules forming the pentagonal bipyramid around calcium are absent and only one O atom of the Glu49 carboxylate group is coordinated to calcium, resulting in only four ligands.

PubMed: 10089353
DOI: 10.1107/S0907444998013699

Experimental method

X-RAY DIFFRACTION (1.9 Å)