Structure of PDB 1e40 Chain A

Receptor sequence
>1e40A (length=483) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
VNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWIPPAYKGLSQS
DNGYGPYDLYDLGEFQQKGTVRTKYGTKSELQDAIGSLHSRNVQVYGDVV
LNHKAGADATEDVTAVEVNPANRNQETSEEYQIKAWTDFRFPGRGNTYSD
FKWHWYHFDGADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYAD
VDYDHPDVVAETKKWGIWYANELSLDGFRIDAAKHIKFSFLRDWVQAVRQ
ATGKEMFTVAEYWQNNAGKLENYLNKTSFNQSVFDVPLHFNLQAASSQGG
GYDMRKLLNGTVVSKHPLKSVTFVDNHDTQPGQSLESTVQTWFKPLAYAF
ILTRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQH
DYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWH
DITGNRSEPVVINSEGWGEFHVNGGSVSIYVQR
3D structure
PDB1e40 Structural Analysis of a Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R229 D231 E261 H327 D328
Catalytic site (residue number reindexed from 1) R229 D231 E261 H327 D328
Enzyme Commision number 3.2.1.1: alpha-amylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e40, PDBe:1e40, PDBj:1e40
PDBsum1e40
PubMed10924103
UniProtP00692|AMY_BACAM Alpha-amylase

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