Structure of PDB 1zwj Chain B

Receptor sequence
>1zwjB (length=299) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
QSPELRKDPVTNRWVIFSPTDFKSSCPFCIECAPELFRVPDHDPNWKLRV
IENLYPALSRNLETRTIVGFGFHDVVIESPVHSIQLSDIDPVGIGDILIA
YKKRINQIAQHDSINYIQVFKNQGASAGASMSHSHSQMMALPVVPPTVSS
RLDGTKDYFEETGKCCLCEAKSKHFVIDESSHFVSVAPFAATYPFEIWII
PKDHSSHFHHLDDVKAVDLGGLLKLMLQKIAKQLNDPPYNYMIHTSPLKV
TESQLPYTHWFLQIVPQLSGVGGFEIGTGCYINPVFPEDVAKVMREVSL
3D structure
PDB1zwj Structure and Mechanism of an ADP-Glucose Phosphorylase from Arabidopsis thaliana
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C63 C66 H133 N173 S181 H184 H186 Q188
Catalytic site (residue number reindexed from 1) C26 C29 H82 N122 S130 H133 H135 Q137
Enzyme Commision number 2.7.7.-
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 ZN B C63 H133 H184 C26 H82 H133
BS02 ZN B C216 C219 H255 H310 C165 C168 H204 H259
Gene Ontology
Molecular Function
GO:0008108 UDP-glucose:hexose-1-phosphate uridylyltransferase activity
GO:0008270 zinc ion binding
GO:0016779 nucleotidyltransferase activity
GO:0017103 UTP:galactose-1-phosphate uridylyltransferase activity
GO:0043531 ADP binding
GO:0046872 metal ion binding
GO:0047345 ribose-5-phosphate adenylyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006006 glucose metabolic process
GO:0006012 galactose metabolic process
GO:0080040 positive regulation of cellular response to phosphate starvation

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Molecular Function
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Biological Process
External links
PDB RCSB:1zwj, PDBe:1zwj, PDBj:1zwj
PDBsum1zwj
PubMed16519510
UniProtQ9FK51|AGLUP_ARATH ADP-glucose phosphorylase (Gene Name=At5g18200)

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