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5LGV

GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose

Summary for 5LGV
Entry DOI10.2210/pdb5lgv/pdb
Related PRD IDPRD_900030
DescriptorAlpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total)
Functional Keywordshydrolase, alpha-glucan biosynthesis, glycoside hydrolase family 13_3, transferase
Biological sourceStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Total number of polymer chains2
Total formula weight159301.35
Authors
Syson, K.,Stevenson, C.E.M.,Mia, F.,Barclay, J.E.,Tang, M.,Gorelik, A.,Rashid, A.M.,Lawson, D.M.,Bornemann, S. (deposition date: 2016-07-08, release date: 2016-08-17, Last modification date: 2024-01-10)
Primary citationSyson, K.,Stevenson, C.E.,Miah, F.,Barclay, J.E.,Tang, M.,Gorelik, A.,Rashid, A.M.,Lawson, D.M.,Bornemann, S.
Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE.
J.Biol.Chem., 291:21531-21540, 2016
Cited by
PubMed: 27531751
DOI: 10.1074/jbc.M116.748160
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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