Structure of PDB 5ifk Chain B

Receptor sequence
>5ifkB (length=293) Species: 284590 (Kluyveromyces lactis NRRL Y-1140) [Search protein sequence]
DINEQRALIKSAHRYISEKLEDHFSSEFLPKALVICGSGLSGISTKIADE
PKPLILSYSTIPGFGELIFGYMNGAPVVLMNGRLHSYEGHSLAETVHPIR
ALHLLGSINVLIVTNAAGGINASFKAGDLMCVYDHINFPGLCGFHPLRGA
NFDEFGPRFLATSDAYDLELRKLLFSKKKELNIERKIHEGTYSYVHGPTF
ESRAESRFLRLAGTDAVGMSTVPEVVTARHCGWRVLALSLITNECVVDPP
ASAHDENPVPIQEGKATHEEVLENSAKASKDVQELIFSVVAEI
3D structure
PDB5ifk Functional and Structural Characterization of Purine Nucleoside Phosphorylase from Kluyveromyces lactis and Its Potential Applications in Reducing Purine Content in Food
ChainB
Resolution1.967 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) S38 H85 Y87 E88 A116 M219 S220 N243 C245 H268
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 B A130 G131 F213 E214 M232 N256 A117 G118 F200 E201 M219 N243
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

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

[Back to BioLiP]