Structure of PDB 1jae Chain A

Receptor sequence
>1jaeA (length=471) Species: 7067 (Tenebrio molitor) [Search protein sequence]
QKDANFASGRNSIVHLFEWKWNDIADECERFLQPQGFGGVQISPPNEYLV
ADGRPWWERYQPVSYIINTRSGDESAFTDMTRRCNDAGVRIYVDAVINHM
TGMNGVGTSGSSADHDGMNYPAVPYGSGDFHSPCEVNNYQDADNVRNCEL
VGLRDLNQGSDYVRGVLIDYMNHMIDLGVAGFRVDAAKHMSPGDLSVIFS
GLKNLNTDYGFADGARPFIYQEVIDLGGEAISKNEYTGFGCVLEFQFGVS
LGNAFQGGNQLKNLANWGPEWGLLEGLDAVVFVDNHDNQRTGGSQILTYK
NPKPYKMAIAFMLAHPYGTTRIMSSFDFTDNDQGPPQDGSGNLISPGIND
DNTCSNGYVCEHRWRQVYGMVGFRNAVEGTQVENWWSNDDNQIAFSRGSQ
GFVAFTNGGDLNQNLNTGLPAGTYCDVISGELSGGSCTGKSVTVGDNGSA
DISLGSAEDDGVLAIHVNAKL
3D structure
PDB1jae Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution.
ChainA
Resolution1.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.1: alpha-amylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A N98 R146 D155 H189 N98 R146 D155 H189
BS02 CL A R183 R321 R183 R321
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031404 chloride ion binding
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005615 extracellular space

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Cellular Component
External links
PDB RCSB:1jae, PDBe:1jae, PDBj:1jae
PDBsum1jae
PubMed9600843
UniProtP56634|AMY_TENMO Alpha-amylase

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