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

Related PRD IDPRD_000415
DescriptorLEUCINE AMINOPEPTIDASE, AMASTATIN, ZINC ION, ... (4 entities in total)
Functional Keywordsalpha-aminoacylpeptide, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceBos taurus (bovine)
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Cellular locationCytoplasm P00727
Total number of polymer chains2
Total molecular weight53573.5
Authors
Kim, H.,Lipscomb, W.N. (deposition date: 1993-03-02, release date: 1994-01-31, Last modification date: 2012-12-12)
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
PubMed: 8357796 (PDB entries with the same primary citation)
DOI: 10.1021/bi00084a011
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.4 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers120.8%12.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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