Structure of PDB 1fxu Chain A

Receptor sequence
>1fxuA (length=278) Species: 9913 (Bos taurus) [Search protein sequence]
GYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEI
PNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVF
RLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGPNEE
RFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETV
AECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDTGKAN
HEEVLEAGKQAAQKLEQFVSLLMASIPV
3D structure
PDB1fxu Calf spleen purine nucleoside phosphorylase: structure of its ternary complex with an N(7)-acycloguanosine inhibitor and a phosphate anion.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S33 H64 H86 Y88 E89 A116 M219 S220 N243 V245 H257
Catalytic site (residue number reindexed from 1) S30 H61 H83 Y85 E86 A113 M216 S217 N240 V242 H251
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 PO4 A G32 S33 R84 H86 N115 S220 G29 S30 R81 H83 N112 S217
BS02 GU7 A Y88 A116 A117 G118 F200 E201 M219 T242 N243 H257 V260 Y85 A113 A114 G115 F197 E198 M216 T239 N240 H251 V254
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006166 purine ribonucleoside salvage
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1fxu, PDBe:1fxu, PDBj:1fxu
PDBsum1fxu
PubMed11134924
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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