Structure of PDB 1b8o Chain A

Receptor sequence
>1b8oA (length=280) Species: 9913 (Bos taurus) [Search protein sequence]
NGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSE
IPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRV
FRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNE
ERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFET
VAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESQ
GKANHEEVLEAGKQAAQKLEQFVSLLMASI
3D structure
PDB1b8o Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis.
ChainA
Resolution1.5 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) S31 H62 H84 Y86 E87 A114 M217 S218 N241 V243 H255
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 R84 H86 N115 S220 G30 S31 R82 H84 N113 S218
BS02 IMH A H86 Y88 A116 G118 F200 E201 M219 N243 H257 V260 H84 Y86 A114 G116 F198 E199 M217 N241 H255 V258 MOAD: Ki=23pM
PDBbind-CN: -logKd/Ki=10.64,Ki=23pM
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:1b8o, PDBe:1b8o, PDBj:1b8o
PDBsum1b8o
PubMed11170405
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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