Structure of PDB 5fak Chain D

Receptor sequence
>5fakD (length=282) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
VKVGIIGGTGFKKVGVRQVTTPFGKPSDTLVEGFVGDVACVVLPRHGKGH
LIPPSEVNYRANVWALKDLGCTHILATTACGSLQEDLVPGDFVVLNQFMD
KTWGRENTFYGSKPDSLKGVLHMPMAEPFCERTRQILIQAARNKSINVYD
KKTMDKSACIHPCVHAEGSAVTINGPRFSTRCESFIHKAMGLDIVNMTLV
PEVSLAREAGLSYASIAIVTDFDCWKSEEEHVCVDMVLEQFRKSVVHVRE
ILLEAVALIGAEDWTKTIEANKALVMSSRQDL
3D structure
PDB5fak Crystal Structure of Schistosoma mansoni Adenosine Phosphorylase/5'-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway.
ChainD
Resolution1.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K34 H59 D230 D232
Catalytic site (residue number reindexed from 1) K25 H50 D221 D223
Enzyme Commision number 2.4.2.28: S-methyl-5'-thioadenosine 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 ADE D A88 C89 G90 F187 V204 N205 M206 D230 D232 A79 C80 G81 F178 V195 N196 M197 D221 D223
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0017061 S-methyl-5-thioadenosine phosphorylase activity
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0009116 nucleoside metabolic process
GO:0019509 L-methionine salvage from methylthioadenosine
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fak, PDBe:5fak, PDBj:5fak
PDBsum5fak
PubMed27935959
UniProtI0B503

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