Structure of PDB 3fuc Chain C

Receptor sequence
>3fucC (length=274) Species: 9913 (Bos taurus) [Search protein sequence]
NGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSE
IPNFPGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLGVET
LVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGVRFP
AMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECRLLR
NLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESQGKANHEEV
LEAGKQAAQKLEQFVSLLMASIPV
3D structure
PDB3fuc 1.45 A resolution crystal structure of recombinant PNP in complex with a pM multisubstrate analogue inhibitor bearing one feature of the postulated transition state.
ChainC
Resolution1.45 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 H86 Y88 E89 A116 M219 S220 N243 V245 H257
Catalytic site (residue number reindexed from 1) S31 H76 Y78 E79 A106 M209 S210 N233 V235 H247
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 9D9 C S33 R84 H86 N115 A116 A117 G118 F200 E201 V217 M219 S220 T242 N243 S31 R74 H76 N105 A106 A107 G108 F190 E191 V207 M209 S210 T232 N233 MOAD: Kd=190pM
BindingDB: IC50=10.2nM,Ki=1nM,Kd=0.1nM
BS02 AZI C P92 K95 P82 K85
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:3fuc, PDBe:3fuc, PDBj:3fuc
PDBsum3fuc
PubMed19944078
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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