Structure of PDB 1a9q Chain A

Receptor sequence
>1a9qA (length=282) Species: 9913 (Bos taurus) [Search protein sequence]
MQNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDY
SEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPV
RVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGP
NEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNF
ETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDTE
SQGKANHEEVLEAGKQAAQKLEQFVSLLMASI
3D structure
PDB1a9q Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues.
ChainA
Resolution2.0 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) S33 H64 H86 Y88 E89 A116 M219 S220 N243 V245 H257
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 HPA A A117 G118 F200 E201 M219 N243 A117 G118 F200 E201 M219 N243 PDBbind-CN: -logKd/Ki=6.17,Kd=0.68uM
BindingDB: Kd=680nM
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1a9q, PDBe:1a9q, PDBj:1a9q
PDBsum1a9q
PubMed9585525
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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