Structure of PDB 5znc Chain A

Receptor sequence
>5zncA (length=242) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
LLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVECH
YKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKRG
DICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGI
SVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGIL
IVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA
3D structure
PDB5znc Identifying purine nucleoside phosphorylase as the target of quinine using cellular thermal shift assay.
ChainA
Resolution1.66 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 QI9 A V66 S91 C92 G93 Y160 V181 E182 M183 D218 V63 S88 C89 G90 Y157 V178 E179 M180 D215 MOAD: Kd=65nM
PDBbind-CN: -logKd/Ki=7.52,Kd=29.9nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0006218 uridine catabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5znc, PDBe:5znc, PDBj:5znc
PDBsum5znc
PubMed30602534
UniProtQ8T9Z7|PNPH_PLAFA Purine nucleoside phosphorylase (Gene Name=PNP)

[Back to BioLiP]