Structure of PDB 1lvu Chain D

Receptor sequence
>1lvuD (length=279) Species: 9913 (Bos taurus) [Search protein sequence]
QNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYS
EIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVR
VFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGPN
EERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFE
TVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYES
QHEEVLEAGKQAAQKLEQFVSLLMASIPV
3D structure
PDB1lvu Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis
ChainD
Resolution2.05 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 Y88 A116 M219 S220 H257
Catalytic site (residue number reindexed from 1) S32 H63 Y87 A115 M218 S219 H252
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 CA D S51 E58 S50 E57
BS02 9PP D G32 S33 H86 N115 A116 A117 G118 F200 E201 M219 S220 N243 G31 S32 H85 N114 A115 A116 G117 F199 E200 M218 S219 N242 MOAD: Kd=4.8uM
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:1lvu, PDBe:1lvu, PDBj:1lvu
PDBsum1lvu
PubMed15342253
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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