Structure of PDB 2qpl Chain A

Receptor sequence

>2qplA (length=266) Species: 9913 (Bos taurus)

NGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSE
IPNFPEGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLL
GVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFG
VRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAEC
RLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYEAGKQAA
QKLEQFVSLLMASIPV

3D structure

• PDB: 2qpl Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S33 H64 H86 Y88 E89 A116 M219 S220 N243 V245
• Catalytic site (residue number reindexed from 1): S31 H58 H80 Y82 E83 A110 M213 S214 N237 V239
• 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	BTY	A	A117 G118 F200 E201 V217 M219 T242 N243	A111 G112 F194 E195 V211 M213 T236 N237	MOAD: ic50=18.9uM

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:2qpl, PDBe:2qpl, PDBj:2qpl
• PDBsum: 2qpl
• PubMed: 17927987
• UniProt: P55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)