Structure of PDB 1lvu Chain F

Receptor sequence
>1lvuF (length=269) Species: 9913 (Bos taurus) [Search protein sequence]
MQNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDY
SEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPV
RVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGP
NEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNF
ETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYE
QAAQKLEQFVSLLMASIPV
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
ChainF
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) S2033 H2064 H2086 Y2088 E2089 A2116 M2219 S2220 N2243 V2245
Catalytic site (residue number reindexed from 1) S33 H64 H86 Y88 E89 A116 M219 S220 N243 V245
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 F S2051 E2058 S51 E58
BS02 9PP F G2032 S2033 H2086 N2115 A2116 A2117 G2118 F2200 E2201 V2217 M2219 S2220 N2243 G32 S33 H86 N115 A116 A117 G118 F200 E201 V217 M219 S220 N243 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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