Structure of PDB 1a9p Chain A

Receptor sequence

>1a9pA (length=289) Species: 9913 (Bos taurus)

MQNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDY
SEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPV
RVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGP
NEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNF
ETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDTE
SQGKANHEEVLEAGKQAAQKLEQFVSLLMASIPVSGHTG

3D structure

• PDB: 1a9p Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues.
• Chain: A
• Resolution: 2.4 Å

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	PO4	A	G32 S33 H64 R84 H86 N115 S220	G32 S33 H64 R84 H86 N115 S220
BS02	9DI	A	H86 Y88 A116 G118 F200 E201 M219 N243 H257 E259	H86 Y88 A116 G118 F200 E201 M219 N243 H257 E259

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

External links

• PDB: RCSB:1a9p, PDBe:1a9p, PDBj:1a9p
• PDBsum: 1a9p
• PubMed: 9585525
• UniProt: P55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)