Structure of PDB 1v48 Chain A

Receptor sequence
>1v48A (length=261) Species: 9913 (Bos taurus) [Search protein sequence]
QNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYS
EIPNFPESGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLG
VETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGV
RFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECR
LLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYEAAQKLEQ
FVSLLMASIPV
3D structure
PDB1v48 Calf spleen purine-nucleoside phosphorylase: crystal structure of the binary complex with a potent multisubstrate analogue inhibitor.
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 H86 Y88 E89 A116 M219 S220 N243 V245
Catalytic site (residue number reindexed from 1) S32 H79 Y81 E82 A109 M212 S213 N236 V238
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 HA1 A S33 R84 H86 A116 G118 F200 E201 V217 M219 S220 N243 S32 R77 H79 A109 G111 F193 E194 V210 M212 S213 N236 MOAD: Ki=16nM
PDBbind-CN: -logKd/Ki=7.80,Ki=16nM
BindingDB: Ki=2.7nM,IC50=18.7nM,Kd=0.46nM
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:1v48, PDBe:1v48, PDBj:1v48
PDBsum1v48
PubMed15272165
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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