Structure of PDB 2q4h Chain B

Receptor sequence
>2q4hB (length=305) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
QSPELRKDPVTNRWVIFSPTDFKSSCPFCIGREQECAPELFRVPDHDPNW
KLRVIENLYPALSRNLETQSRTIVGFGFHDVVIESPVHSIQLSDIDPVGI
GDILIAYKKRINQIAQHDSINYIQVFKNQGASAGASMSHSHSQMMALPVV
PPTVSSRLDGTKDYFEETGKCCLCEAKSKHFVIDESSHFVSVAPFAATYP
FEIWIIPKDHSSHFHHLDDVKAVDLGGLLKLMLQKIAKQLNDPPYNYMIH
TSPLKVTESQLPYTHWFLQIVPQLSGVGGFEIGTGCYINPVFPEDVAKVM
REVSL
3D structure
PDB2q4h Ensemble refinement of protein crystal structures: validation and application.
ChainB
Resolution1.834 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 H88 N128 S136 H139 H141 Q143
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 C66 H133 H184 C26 C29 H88 H139
BS02 ZN B C216 C219 H255 C171 C174 H210
BS03 AMP B A74 N94 L95 Y96 A180 S181 M182 H186 Q188 A37 N57 L58 Y59 A135 S136 M137 H141 Q143
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:2q4h, PDBe:2q4h, PDBj:2q4h
PDBsum2q4h
PubMed17850744
UniProtQ9FK51|AGLUP_ARATH ADP-glucose phosphorylase (Gene Name=At5g18200)

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