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9US3

Klebsiella pneumoniae maltohexaose-producing alpha-amylase

Summary for 9US3
Entry DOI10.2210/pdb9us3/pdb
DescriptorMaltohexaose-producing amylase, CALCIUM ION (3 entities in total)
Functional Keywordsglycosyl hydrolase family 13, hydrolase
Biological sourceKlebsiella pneumoniae
Total number of polymer chains2
Total formula weight148702.17
Authors
Fujimoto, Z.,Kishine, N.,Momma, M. (deposition date: 2025-05-01, release date: 2025-07-09)
Primary citationFujimoto, Z.,Kishine, N.,Momma, M.
Crystal structure of Klebsiella pneumoniae maltohexaose-producing alpha-amylase.
J.Biochem., 2025
Cited by
PubMed Abstract: The α-amylase from Klebsiella pneumoniae (KpAmy13), which belongs to glycoside hydrolase family 13 subfamily 19, produces maltohexaose as an initial product when acting on starch and has been characterized as a maltohexaose-producing α-amylase. The crystal structure of KpAmy13 was determined at a resolution of 1.9 Å, revealing the structures of all its domains: N, A, B, and C. Domain N resembles the starch-binding domain known as carbohydrate-binding module family 69, found in α-glucan-related proteins. Although domain N does not conserve the starch-binding residues observed in other proteins, it has several hydrophobic residues on its surface, which might be involved in promoting catalysis. The catalytic cleft is located at the bottom of a circular depression. The domain N-truncated mutant of KpAmy13 in complex with maltohexaose showed that its non-reducing end glucose docks at subsite -6. The long and complex structure of domain B contributes to forming a cleft of the right size for six glucose moieties, demonstrating the exo-acting mechanism.
PubMed: 40576559
DOI: 10.1093/jb/mvaf034
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.899 Å)
Structure validation

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数据于2025-07-09公开中

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