Structure of PDB 1yp4 Chain A

Receptor sequence
>1yp4A (length=432) Species: 4113 (Solanum tuberosum) [Search protein sequence]
TCLDPDASRSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVS
NCLNSNISKIYVLTQFNSASLNRHLSRAYAGFVEVLAAQQSPENPDWFQG
TADAVRQYLWLFEEHTVLEYLILAGDHLYRMDYEKFIQAHRETDADITVA
ALPMDEKRATAFGLMKIDEEGRIIEFAEKPQGEQLQAMKVDTTILGLDDK
RAKEMPFIASMGIYVISKDVMLNLLRDKFPGANDFGSEVIPGATSLGMRV
QAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLP
PSKMLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGA
DYYETDADRKLLAAKGSVPIGIGKNCHIKRAIIDKNARIGDNVKIINKDN
VQEAARETDGYFIKSGIVTVIKDALIPSGIII
3D structure
PDB1yp4 Crystal structure of potato tuber ADP-glucose pyrophosphorylase.
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.27: glucose-1-phosphate adenylyltransferase.
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 ADP A L26 G28 G29 Q118 T120 D145 G255 S256 L16 G18 G19 Q99 T101 D126 G236 S237
Gene Ontology
Molecular Function
GO:0008878 glucose-1-phosphate adenylyltransferase activity
Biological Process
GO:0005978 glycogen biosynthetic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1yp4, PDBe:1yp4, PDBj:1yp4
PDBsum1yp4
PubMed15692569
UniProtP23509|GLGS_SOLTU Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic

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