Structure of PDB 5etj Chain F

Receptor sequence
>5etjF (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
TLMENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIF
DYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTF
PVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLR
GPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGP
SFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMD
YESLEKANHDEVAAAGKQAAQKLEQFVSILMASIPLPD
3D structure
PDB5etj Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.
ChainF
Resolution2.3 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 H64 H86 Y88 E89 A116 M219 S220 N243 V245 H257
Catalytic site (residue number reindexed from 1) S35 H66 H88 Y90 E91 A118 M221 S222 N245 V247 H259
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 IM5 F Y88 A116 G118 F200 E201 M219 N243 H257 Y90 A118 G120 F202 E203 M221 N245 H259 MOAD: Kd=66pM
BindingDB: Ki=7nM
Gene Ontology
Molecular Function
GO:0001882 nucleoside binding
GO:0002060 purine nucleobase binding
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0005515 protein binding
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0042301 phosphate ion binding
GO:0042802 identical protein binding
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0000255 allantoin metabolic process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006148 inosine catabolic process
GO:0006149 deoxyinosine catabolic process
GO:0006157 deoxyadenosine catabolic process
GO:0006166 purine ribonucleoside salvage
GO:0006204 IMP catabolic process
GO:0006738 nicotinamide riboside catabolic process
GO:0006955 immune response
GO:0009116 nucleoside metabolic process
GO:0009165 nucleotide biosynthetic process
GO:0009410 response to xenobiotic stimulus
GO:0032743 positive regulation of interleukin-2 production
GO:0034418 urate biosynthetic process
GO:0042102 positive regulation of T cell proliferation
GO:0043101 purine-containing compound salvage
GO:0046059 dAMP catabolic process
GO:0046638 positive regulation of alpha-beta T cell differentiation
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5etj, PDBe:5etj, PDBj:5etj
PDBsum5etj
PubMed26927977
UniProtP00491|PNPH_HUMAN Purine nucleoside phosphorylase (Gene Name=PNP)

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