Structure of PDB 2ai3 Chain A

Receptor sequence
>2ai3A (length=272) Species: 9913 (Bos taurus) [Search protein sequence]
NGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSE
IPNFPESGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLGV
ETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGVR
FPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECRL
LRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYKANHEEVLE
AGKQAAQKLEQFVSLLMASIPV
3D structure
PDB2ai3 Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S33 H86 Y88 E89 A116 M219 S220 N243 V245 H257
Catalytic site (residue number reindexed from 1) S31 H78 Y80 E81 A108 M211 S212 N235 V237 H245
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 P2G A S33 H86 N115 A116 A117 G118 F200 E201 M219 S220 N243 S31 H78 N107 A108 A109 G110 F192 E193 M211 S212 N235 MOAD: ic50=5000nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:2ai3, PDBe:2ai3, PDBj:2ai3
PDBsum2ai3
PubMed16239721
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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