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2C3G

Structure of CBM26 from Bacillus halodurans amylase

Summary for 2C3G
Entry DOI10.2210/pdb2c3g/pdb
Related2C3H 2C3V 2C3W 2C3X
DescriptorALPHA-AMYLASE G-6, CADMIUM ION (3 entities in total)
Functional Keywordscarbohydrate-binding module, starch binding, carbohydrate binding, glycoside hydrolase, amylose, amylopectin, malto-oligosaccharide
Biological sourceBACILLUS HALODURANS
Total number of polymer chains1
Total formula weight11913.04
Authors
Boraston, A.B.,Healey, M.,Klassen, J.,Ficko-Blean, E.,Lammerts Van Bueren, A.,Law, V. (deposition date: 2005-10-07, release date: 2005-10-17, Last modification date: 2011-07-13)
Primary citationBoraston, A.B.,Healey, M.,Klassen, J.,Ficko-Blean, E.,Lammerts Van Bueren, A.,Law, V.
A Structural and Functional Analysis of Alpha-Glucan Recognition by Family 25 and 26 Carbohydrate-Binding Modules Reveals a Conserved Mode of Starch Recognition
J.Biol.Chem., 281:587-, 2006
Cited by
PubMed: 16230347
DOI: 10.1074/JBC.M509958200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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