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PDBe Entry: 1e43 view

NATIVE STRUCTURE OF CHIMAERIC AMYLASE FROM B. AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.7A
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.7 Å, R-factor: 13.3%, Free R-factor: 18.5%, Spacegroup: C 2 2 21
Released 21/06/2001, deposition: 27/06/2000, last revision: 24/02/2009
Authors Brzozowski, A.M.search; Lawson, D.M.search; Turkenburg, J.P.search; Bisgaard-Frantzen, H.search; Svendsen, A.search; Borchert, T.V.search; Dauter, Z.search; Wilson, K.S.search; Davies, G.J.search
Primary citation Structural Analysis of a Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes
BIOCHEMISTRYsearch vol:39, pag:9099 (2000) [PubMed ID 10924103 ]search
Keywords HYDROLASEsearch, AMYLASEsearch, FAMILY 13search
EC 3.2.1.1 ExPASy BRENDA search (A)
Organism Bacillus amyloliquefaciens 1390search(A)
UniProt Alpha-amylase precursor (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) P00692search (A)
Solvent A
Related entries 1vjs, 1bpl, 1bli, 1e3z, 1e40, 1e3x
Polymers
Id Name Type UniProt Residues Observed
A ALPHA-AMYLASE Protein P00692 (AMY_BACAM)search
483 100%
Heterogens
Id Name Ligands
A CALCIUM ION CA search
A SODIUM ION NA search
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