Structure of PDB 1b0i Chain A

Receptor sequence
>1b0iA (length=447) Species: 228 (Pseudoalteromonas haloplanktis) [Search protein sequence]
TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRY
QPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAG
NSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASN
YVQNTIAAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQE
VIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGF
MPSSSAVVFVDNHDNQRGGGAGNVITFEDGRLYDLANVFMLAYPYGYPKV
MSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRNN
TADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQY
CNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLN
3D structure
PDB1b0i Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.
ChainA
Resolution2.4 Å
3D
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
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
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004556 alpha-amylase activity
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1b0i, PDBe:1b0i, PDBj:1b0i
PDBsum1b0i
PubMed9862804
UniProtP29957|AMY_PSEHA Alpha-amylase (Gene Name=amy)

[Back to BioLiP]