Structure of PDB 1a9t Chain A

Receptor sequence
>1a9tA (length=284) Species: 9913 (Bos taurus) [Search protein sequence]
MANGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDY
SEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPV
RVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGP
NEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNF
ETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDTE
SQGKANHEEVLEAGKQAAQKLEQFVSLLMASIPV
3D structure
PDB1a9t 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 R1P A S33 R84 H86 Y88 N115 A116 F200 M219 S220 V260 S33 R84 H86 Y88 N115 A116 F200 M219 S220 V260
BS02 HPA A A116 A117 G118 F200 E201 V217 N243 A116 A117 G118 F200 E201 V217 N243 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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Biological Process
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Cellular Component
External links
PDB RCSB:1a9t, PDBe:1a9t, PDBj:1a9t
PDBsum1a9t
PubMed9585525
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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