Structure of PDB 1e3x Chain A

Receptor sequence
>1e3xA (length=483) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
VNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWIPPAYKGLSQS
DNGYGPYDLYDLGEFQQKGTVRTKYGTKSELQDAIGSLHSRNVQVYGDVV
LNHKAGADATEDVTAVEVNPANRNQETSEEYQIKAWTDFRFPGRGNTYSD
FKWHWYHFDGADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYAD
VDYDHPDVVAETKKWGIWYANELSLDGFRIDAAKHIKFSFLRDWVQAVRQ
ATGKEMFTVAEYWQNNAGKLENYLNKTSFNQSVFDVPLHFNLQAASSQGG
GYDMRKLLNGTVVSKHPLKSVTFVDNHDTQPGQSLESTVQTWFKPLAYAF
ILTRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQH
DYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWH
DITGNRSEPVVINSEGWGEFHVNGGSVSIYVQR
3D structure
PDB1e3x Structural Analysis of a Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
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 N102 D194 D200 H235 N102 D194 D200 H235
BS02 CA A D159 A181 D183 D202 D204 D159 A181 D183 D202 D204
BS03 CA A N444 E447 N444 E447
BS04 CA A G300 Y302 H406 D407 D430 G300 Y302 H406 D407 D430
BS05 NA A D159 D183 D194 D200 V201 D202 D159 D183 D194 D200 V201 D202
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1e3x, PDBe:1e3x, PDBj:1e3x
PDBsum1e3x
PubMed10924103
UniProtP00692|AMY_BACAM Alpha-amylase

[Back to BioLiP]