1E40

Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A

Summary for 1E40

Related1VJS 1BPL 1BLI 1E3X 1E3Z 1E43
DescriptorALPHA-AMYLASE, CALCIUM ION, SODIUM ION, ... (6 entities in total)
Functional Keywordshydrolase, amylase, family 13, maltotriose, tris, complex
Biological sourceBACILLUS AMYLOLIQUEFACIENS
Total number of polymer chains1
Total molecular weight55884.32
Authors
Brzozowski, A.M.,Lawson, D.M.,Turkenburg, J.P.,Bisgaard-Frantzen, H.,Svendsen, A.,Borchert, T.V.,Dauter, Z.,Wilson, K.S.,Davies, G.J. (deposition date: 2000-06-27, release date: 2001-06-21, Last modification date: 2019-05-08)
Primary citation
Brzozowski, A.M.,Lawson, D.M.,Turkenburg, J.P.,Bisgaard-Frantzen, H.,Svendsen, A.,Borchert, T.V.,Dauter, Z.,Wilson, K.S.,Davies, G.J.
Structural Analysis of a Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes
Biochemistry, 39:9099-, 2000
PubMed: 10924103 (PDB entries with the same primary citation)
DOI: 10.1021/BI0000317
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers4 0.2% 2.7% 0.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report