Structure of PDB 3phc Chain E

Receptor sequence
>3phcE (length=243) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVEC
HYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKR
GDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNG
ISVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI
LIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA
3D structure
PDB3phc Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG
ChainE
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H7 G23 R27 R45 E77 R88 S91 D206 G207 P209 V222
Catalytic site (residue number reindexed from 1) H5 G21 R25 R43 E75 R86 S89 D204 G205 P207 V220
Enzyme Commision number 2.4.2.1: purine-nucleoside phosphorylase.
2.4.2.44: S-methyl-5'-thioinosine phosphorylase.
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 IM5 E S91 C92 G93 Y160 V181 E182 M183 E184 D206 W212 S89 C90 G91 Y158 V179 E180 M181 E182 D204 W210
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0017061 S-methyl-5-thioadenosine phosphorylase activity
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006148 inosine catabolic process
GO:0006166 purine ribonucleoside salvage
GO:0006195 purine nucleotide catabolic process
GO:0006218 uridine catabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3phc, PDBe:3phc, PDBj:3phc
PDBsum3phc
PubMed
UniProtQ8I3X4|PNPH_PLAF7 Purine nucleoside phosphorylase (Gene Name=PNP)

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