Structure of PDB 1nw4 Chain E

Receptor sequence

>1nw4E (length=243) Species: 36329 (Plasmodium falciparum 3D7)

NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVEC
HYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKR
GDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNG
ISVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI
LIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA

3D structure

• PDB: 1nw4 Plasmodium falciparum Purine Nucleoside Phosphorylase: CRYSTAL STRUCTURES, IMMUCILLIN INHIBITORS, AND DUAL CATALYTIC FUNCTION.
• Chain: E
• Resolution: 2.2 Å

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	IMH	E	S91 C92 G93 Y160 E182 M183 E184 D206	S89 C90 G91 Y158 E180 M181 E182 D204	MOAD: Kd=0.86nM

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

External links

• PDB: RCSB:1nw4, PDBe:1nw4, PDBj:1nw4
• PDBsum: 1nw4
• PubMed: 14982926
• UniProt: Q8I3X4|PNPH_PLAF7 Purine nucleoside phosphorylase (Gene Name=PNP)