BioLiP

Structure of PDB 1tcu Chain C

Receptor sequence

>1tcuC (length=285) Species: 6183 (Schistosoma mansoni) [Search protein sequence]

ESVTANIENVKKVAHHIQKLTSIVPEIGIICGSGLGKLADGVKDKITIPY
TKIPNFPQTSVVGHSGNLIFGTLSGRKVVVMQGRFHMYEGYSNDTVALPI
RVMKLLGVKILMVSNAAGGLNRSLKLGDFVILKDHIYLPGLGLNNILVGP
NQEAFGTRFPALSNAYDRDLRKLAVQVAEENGFGNLVHQGVYVMNGGPCY
ETPAECTMLLNMGCDVVGMSTIPEVVIARHCGIQVFAVSLVTNISVLDVE
SDLKPNHEEVLATGAQRAELMQSWFEKIIEKLPKD

3D structure

PDB

1tcu Structures for the Potential Drug Target Purine Nucleoside Phosphorylase from Schistosoma mansoni Causal Agent of Schistosomiasis.

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	S35 H66 H88 Y90 E91 A118 M221 S222 N245 S247 H259
Catalytic site (residue number reindexed from 1)	S33 H64 H86 Y88 E89 A116 M219 S220 N243 S245 H257
Enzyme Commision number	2.4.2.1: purine-nucleoside 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	ACT	C	A119 G120 E203 V219 N245	A117 G118 E201 V217 N243
BS02	PO4	C	G34 R86 H88 N117 S222	G32 R84 H86 N115 S220

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004731	purine-nucleoside phosphorylase activity
GO:0016757	glycosyltransferase activity
GO:0047975	guanosine phosphorylase activity

	Biological Process
GO:0006139	nucleobase-containing compound metabolic process
GO:0009116	nucleoside metabolic process

	Cellular Component
GO:0005737	cytoplasm

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Molecular Function

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Biological Process

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Cellular Component

PDB	RCSB:1tcu, PDBe:1tcu, PDBj:1tcu
PDBsum	1tcu
PubMed	16182308
UniProt	Q9BMI9