Structure of PDB 1z84 Chain A

Receptor sequence
>1z84A (length=311) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
SPELRKDPVTNRWVIFSPRPTDFKSKSPSSCPFCIGREQECAPELFRVPD
HDPNWKLRVIENLYPALSRNLETQSRTIVGFGFHDVVIESPVHSIQLSDI
DPVGIGDILIAYKKRINQIAQHDSINYIQVFKNQGASAGASMSHSHSQMM
ALPVVPPTVSSRLDGTKDYFEETGKCCLCEAKSKHFVIDESSHFVSVAPF
AATYPFEIWIIPKDHSSHFHHLDDVKAVDLGGLLKLMLQKIAKQLNDPPY
NYMIHTSPLKVTESQLPYTHWFLQIVPQLSGVGGFEIGTGCYINPVFPED
VAKVMREVSLT
3D structure
PDB1z84 Structure and Mechanism of an ADP-Glucose Phosphorylase from Arabidopsis thaliana
ChainA
Resolution1.83 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) C31 C34 H93 N133 S141 H144 H146 Q148
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 A C63 C66 H133 H184 C31 C34 H93 H144
BS02 ZN A C216 C219 H255 H310 C176 C179 H215 H270
BS03 AMP A F65 N94 L95 Y96 N173 A180 S181 M182 H186 Q188 F33 N62 L63 Y64 N133 A140 S141 M142 H146 Q148
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:1z84, PDBe:1z84, PDBj:1z84
PDBsum1z84
PubMed16519510
UniProtQ9FK51|AGLUP_ARATH ADP-glucose phosphorylase (Gene Name=At5g18200)

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