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
PDB1tcu Structures for the Potential Drug Target Purine Nucleoside Phosphorylase from Schistosoma mansoni Causal Agent of Schistosomiasis.
ChainC
Resolution2.0 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
External links
PDB RCSB:1tcu, PDBe:1tcu, PDBj:1tcu
PDBsum1tcu
PubMed16182308
UniProtQ9BMI9

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