Structure of PDB 5fak Chain B

Receptor sequence
>5fakB (length=286) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
KVKVGIIGGTGFDDPNLFKKVGVRQVTTPFGKPSDTLVEGFVGDVACVVL
PRHGKGHLIPPSEVNYRANVWALKDLGCTHILATTACGSLQEDLVPGDFV
VLNQFMDKTWGRENTFYGSKPDSLKGVLHMPMAEPFCERTRQILIQAARN
KSINVYDKKTMDKSACIHPCVHAEGSAVTINGPRFSTRCESFIHKAMGLD
IVNMTLVPEVSLAREAGLSYASIAIVTDFDCWKEHVCVDMVLEQFRKSVV
HVREILLEAVALIGAEDWTKTIEANKALVMSSRQDL
3D structure
PDB5fak Crystal Structure of Schistosoma mansoni Adenosine Phosphorylase/5'-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway.
ChainB
Resolution1.87 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) K34 H59 D230 D232
Catalytic site (residue number reindexed from 1) K32 H57 D228 D230
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 B A88 C89 G90 F187 V204 A86 C87 G88 F185 V202
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

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

[Back to BioLiP]