1LCL
CHARCOT-LEYDEN CRYSTAL PROTEIN
Summary for 1LCL
Entry DOI | 10.2210/pdb1lcl/pdb |
Descriptor | LYSOPHOSPHOLIPASE (2 entities in total) |
Functional Keywords | charcot-leyden crystal protein, serine esterase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasmic granule: Q05315 |
Total number of polymer chains | 1 |
Total formula weight | 16499.89 |
Authors | Acharya, K.R.,Leonidas, D.D. (deposition date: 1996-01-18, release date: 1997-01-11, Last modification date: 2024-02-14) |
Primary citation | Leonidas, D.D.,Elbert, B.L.,Zhou, Z.,Leffler, H.,Ackerman, S.J.,Acharya, K.R. Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure, 3:1379-1393, 1995 Cited by PubMed: 8747464DOI: 10.1016/S0969-2126(01)00275-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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