Structure of PDB 1sq6 Chain A

Receptor sequence

>1sq6A (length=225) Species: 36329 (Plasmodium falciparum 3D7)

LLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVECH
YKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKRG
DICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGI
SVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGIL
IVDGHQLENMIKIALGACAKLATKY

3D structure

• PDB: 1sq6 Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H15 G31 R35 R53 E85 R96 S99 D214 G215
• Catalytic site (residue number reindexed from 1): H4 G20 R24 R42 E74 R85 S88 D203 G204
• 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	SO4	A	G31 R96 S99	G20 R85 S88

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:1sq6, PDBe:1sq6, PDBj:1sq6
• PDBsum: 1sq6
• PubMed: 16131758
• UniProt: Q8I3X4|PNPH_PLAF7 Purine nucleoside phosphorylase (Gene Name=PNP)