Structure of PDB 3fow Chain B

Receptor sequence

>3fowB (length=233) Species: 36329 (Plasmodium falciparum 3D7)

NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVEC
HYKGQKFLCVSHGIGSAGCAICFEELCQNGAKVIIRAGSCGSLQPDLIKR
GDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNG
ISVSSDMFYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI
LIVDGCPFLVPHQLENMIKIALGACAKLATKYA

3D structure

• PDB: 3fow Structural determinants of the 5'-methylthioinosine specificity of Plasmodium purine nucleoside phosphorylase.
• Chain: B
• Resolution: 2.8 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 V210
• 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	B	I66 S91 C92 G93 F160 E182 M183 E184 D206	I64 S89 C90 G91 F158 E180 M181 E182 D204

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:3fow, PDBe:3fow, PDBj:3fow
• PDBsum: 3fow
• PubMed: 24416224
• UniProt: Q8I3X4|PNPH_PLAF7 Purine nucleoside phosphorylase (Gene Name=PNP)