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Ligands
Code Name Style Show Link
CA Calcium ion
CL Chloride ion
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
Code Name Show
PCA Pyroglutamic acid
Glycosylation
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Code : 5TD4   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Starch binding sites on the Human pancreatic alpha amylase D300N variant complexed with an octaose substrate.
Release Data : 2016-11-02
Compound :
mol_id molecule chains synonym
1 Pancreatic alpha-amylase A PA,1,4-alpha-D-glucan glucanohydrolase
ec: 3.2.1.1
fragment: UNP residues 16-511
mutation: D300N
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Komagataella pastoris  (taxid:4922)
organ: Pancreas
gene: AMY2A
Authors : Caner, S., Brayer, G.D.
Keywords : Amylase, Diabetes, Obesity, Glucosyl hydrolase, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.300 Å )
Citation :

Evaluation of the Significance of Starch Surface Binding Sites on Human Pancreatic alpha-Amylase.

Zhang, X.,Caner, S.,Kwan, E.  et al.
(2016)  Biochemistry  55 : 6000 - 6009

PubMed: 27756128
DOI: 10.1021/acs.biochem.6b00992

Chain : A
UniProt : P04746 (AMYP_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D- glucose units. 3.2.1.1 PubMed:10091666, PubMed:10769135, PubMed:11772019, PubMed:11914097
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