Structure of PDB 5i3c Chain A

Receptor sequence
>5i3cA (length=237) Species: 331111 (Escherichia coli O139:H28 str. E24377A) [Search protein sequence]
ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
3D structure
PDB5i3c Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.
ChainA
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H4 G20 R24 R43 E75 R87 S90 S203 D204 I206 R217
Catalytic site (residue number reindexed from 1) H4 G20 R24 R43 E75 R87 S90 S203 D204 I206 R217
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 AC2 A S90 C91 G92 F159 V178 E179 I206 S90 C91 G92 F159 V178 E179 I206
BS02 SO4 A G20 R87 G89 S90 G20 R87 G89 S90
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:0006152 purine nucleoside catabolic process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0042278 purine nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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External links
PDB RCSB:5i3c, PDBe:5i3c, PDBj:5i3c
PDBsum5i3c
PubMed29969103
UniProtA7ZVS7|DEOD_ECO24 Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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