Structure of PDB 1bag Chain A

Receptor sequence
>1bagA (length=425) Species: 1423 (Bacillus subtilis) [Search protein sequence]
LTAPSIKSGTILHAWNWSFNTLKHNMKDIHDAGYTAIQTSPINQVKEGNQ
GDKSMSNWYWLYQPTSYQIGNRYLGTEQEFKEMCAAAEEYGIKVIVDAVI
NHTTFDYAAISNEVKSIPNWTHGNTQIKNWSDRWDVTQNSLLGLYDWNTQ
NTQVQSYLKRFLERALNDGADGFRFDAAKHIELPDDGSYGSQFWPNITNT
SAEFQYGQILQDSASRDAAYANYMDVTASNYGHSIRSALKNRNLGVSNIS
HYASDVSADKLVTWVESHDTYANDDEESTWMSDDDIRLGWAVIASRSGST
PLFFSRPEGGGNGVRFPGKSQIGDRGSALFEDQAITAVNRFHNVMAGQPE
ELSNPNGNNQIFMNQRGSHGVVLANAGSSSVSINTATKLPDGRYDNKAGA
GSFQVNDGKLTGTINARSVAVLYPD
3D structure
PDB1bag Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose.
ChainA
Resolution2.5 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 BGC A W130 K179 L210 W130 K179 L210
BS02 GLC A A177 H180 Q208 A177 H180 Q208
BS03 GLC A W58 H102 D176 Q208 H268 D269 W58 H102 D176 Q208 H268 D269
BS04 GLC A W58 Y59 Q63 L142 N273 W58 Y59 Q63 L142 N273
BS05 GLC A F105 L142 F105 L142
BS06 CA A N101 T137 D146 H180 N101 T137 D146 H180
BS07 CA A G169 D171 G169 D171
BS08 CA A E276 G313 E276 G313
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004556 alpha-amylase activity
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1bag, PDBe:1bag, PDBj:1bag
PDBsum1bag
PubMed9514750
UniProtP00691|AMY_BACSU Alpha-amylase (Gene Name=amyE)

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