Structure of PDB 1kxh Chain A

Receptor sequence
>1kxhA (length=448) Species: 228 (Pseudoalteromonas haloplanktis) [Search protein sequence]
TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRY
QPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAG
NSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASN
YVQNTIAAYINDLQAIGVKGFRFNASKHVAASDIQSLMAKVNGSPVVFQE
VIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGF
MPSSSAVVFVDNHDNQRGHGGAGNVITFEDGRLYDLANVFMLAYPYGYPK
VMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRN
NTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQ
YCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLN
3D structure
PDB1kxh Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase.
ChainA
Resolution2.3 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 GLC A Y50 H89 N174 A175 E200 D264 Y50 H89 N174 A175 E200 D264
BS02 GLC A W46 W47 Q51 H269 W46 W47 Q51 H269
BS03 AC1 A W47 Q51 V140 W47 Q51 V140
BS04 CA A N88 Q135 D144 H178 N88 Q135 D144 H178
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:1kxh, PDBe:1kxh, PDBj:1kxh
PDBsum1kxh
PubMed11914073
UniProtP29957|AMY_PSEHA Alpha-amylase (Gene Name=amy)

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