1BLL
X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE
Summary for 1BLL
Entry DOI | 10.2210/pdb1bll/pdb |
Related PRD ID | PRD_000415 |
Descriptor | LEUCINE AMINOPEPTIDASE, AMASTATIN, ZINC ION, ... (4 entities in total) |
Functional Keywords | alpha-aminoacylpeptide, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Bos taurus (bovine) More |
Cellular location | Cytoplasm: P00727 |
Total number of polymer chains | 2 |
Total formula weight | 53573.50 |
Authors | Kim, H.,Lipscomb, W.N. (deposition date: 1993-03-02, release date: 1994-01-31, Last modification date: 2023-11-15) |
Primary citation | Kim, H.,Lipscomb, W.N. X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state. Biochemistry, 32:8465-8478, 1993 Cited by PubMed: 8357796DOI: 10.1021/bi00084a011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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