Structure of PDB 2isc Chain E

Receptor sequence
>2iscE (length=229) Species: 5722 (Trichomonas vaginalis) [Search protein sequence]
ATPHNSAQVGDFAETVLMCGDPLRAKLIAETYLENPKLVNNVRGIQGYTG
TYKGKPISVMGHGMGLPSICIYAEELYSTYKVKTIIRVGTCGAIDMDIHT
RDIVIFTSAGTNSKINRIRFMDHDYPATASFDVVCALVDAAKELNIPAKV
GKGFSTDLFYNPQTELAQLMNKFHFLAVEMESAGLFPIADLYGARAGCIC
TVSDHILHHERQNSFQNMMKIALEAAIKL
3D structure
PDB2isc Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues
ChainE
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H4 G20 R24 R43 E75 R87 T90 S203 D204 I206 R217
Catalytic site (residue number reindexed from 1) H4 G20 R24 R43 E75 R87 T90 S203 D204 I206 R211
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 223 E M64 T90 C91 G92 F159 V178 M180 E181 D204 M64 T90 C91 G92 F159 V178 M180 E181 D204
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0004850 uridine phosphorylase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006218 uridine catabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2isc, PDBe:2isc, PDBj:2isc
PDBsum2isc
PubMed17223688
UniProtA2E7Y6

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