Structure of PDB 1l0p Chain A

Receptor sequence
>1l0pA (length=448) Species: 228 (Pseudoalteromonas haloplanktis) [Search protein sequence]
TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRY
QPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAG
NSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASN
YVQNTIAAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQE
VIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGF
MPSSSAVVFVDNHDNQRGHGGAGNVITFEDGRLYDLANVFMLAYPYGYPK
VMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRN
NTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQ
YCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLN
3D structure
PDB1l0p Structural basis of alpha-amylase activation by chloride.
ChainA
Resolution2.1 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 CA A N88 Q135 D144 H178 N88 Q135 D144 H178
BS02 NO3 A R172 F259 N262 K300 R172 F259 N262 K300
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:1l0p, PDBe:1l0p, PDBj:1l0p
PDBsum1l0p
PubMed12021442
UniProtP29957|AMY_PSEHA Alpha-amylase (Gene Name=amy)

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