1MKS
CARBOXYLIC ESTER HYDROLASE, TRIGONAL FORM OF THE TRIPLE MUTANT
Summary for 1MKS
Entry DOI | 10.2210/pdb1mks/pdb |
Descriptor | PHOSPHOLIPASE A2, CALCIUM ION (3 entities in total) |
Functional Keywords | hydrolase, enzyme, carboxylic ester hydrolase, trigonal form |
Biological source | Bos taurus (cattle) |
Cellular location | Secreted: P00593 |
Total number of polymer chains | 1 |
Total formula weight | 13817.60 |
Authors | Sundaralingam, M. (deposition date: 1997-08-27, release date: 1997-12-24, Last modification date: 2024-04-03) |
Primary citation | Sekar, K.,Yu, B.Z.,Rogers, J.,Lutton, J.,Liu, X.,Chen, X.,Tsai, M.D.,Jain, M.K.,Sundaralingam, M. Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99. Biochemistry, 36:3104-3114, 1997 Cited by PubMed: 9115986DOI: 10.1021/bi961576x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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