Structure of PDB 1g9h Chain A

Receptor sequence
>1g9hA (length=448) Species: 228 (Pseudoalteromonas haloplanktis) [Search protein sequence]
TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRY
QPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAG
NSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASN
YVQNTIAAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQE
VIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGF
MPSSSAVVFVDNHDNQRGHGGAGNVITFEDGRLYDLANVFMLAYPYGYPK
VMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRN
NTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQ
YCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLN
3D structure
PDB1g9h Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase.
ChainA
Resolution1.8 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 K177 E207 K177 E207
BS02 DAF A W46 Y50 H89 D174 A175 H178 E200 H263 D264 W46 Y50 H89 D174 A175 H178 E200 H263 D264
BS03 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
View graph for
Biological Process
External links
PDB RCSB:1g9h, PDBe:1g9h, PDBj:1g9h
PDBsum1g9h
PubMed11914073
UniProtP29957|AMY_PSEHA Alpha-amylase (Gene Name=amy)

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