Structure of PDB 5ifk Chain C

Receptor sequence
>5ifkC (length=292) Species: 284590 (Kluyveromyces lactis NRRL Y-1140) [Search protein sequence]
INEQRALIKSAHRYISEKLEDHFSSEFLPKALVICGSGLSGISTKIADEP
KPLILSYSTIPGFGELIFGYMNGAPVVLMNGRLHSYEGHSLAETVHPIRA
LHLLGSINVLIVTNAAGGINASFKAGDLMCVYDHINFPGLCGFHPLRGAN
FDEFGPRFLATSDAYDLELRKLLFSKKKELNIERKIHEGTYSYVHGPTFE
SRAESRFLRLAGTDAVGMSTVPEVVTARHCGWRVLALSLITNECVVDPPA
SAHDENPVPIQEGKATHEEVLENSAKASKDVQELIFSVVAEI
3D structure
PDB5ifk Functional and Structural Characterization of Purine Nucleoside Phosphorylase from Kluyveromyces lactis and Its Potential Applications in Reducing Purine Content in Food
ChainC
Resolution1.967 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S42 H98 Y100 E101 A129 M232 S233 N256 C258 H281
Catalytic site (residue number reindexed from 1) S37 H84 Y86 E87 A115 M218 S219 N242 C244 H267
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 HPA C A130 G131 F213 E214 V230 M232 T255 N256 A116 G117 F199 E200 V216 M218 T241 N242
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ifk, PDBe:5ifk, PDBj:5ifk
PDBsum5ifk
PubMed27768715
UniProtQ6CSZ6

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