Structure of PDB 5i3c Chain C

Receptor sequence

>5i3cC (length=237) Species: 331111 (Escherichia coli O139:H28 str. E24377A)

ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK

3D structure

• PDB: 5i3c Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.
• Chain: C
• Resolution: 2.32 Å

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	C	M64 S90 C91 G92 F159 V178 E179 M180	M64 S90 C91 G92 F159 V178 E179 M180
BS02	SO4	C	G20 R87 S90	G20 R87 S90
BS03	SO4	C	T219 N222	T219 N222

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

External links

• PDB: RCSB:5i3c, PDBe:5i3c, PDBj:5i3c
• PDBsum: 5i3c
• PubMed: 29969103
• UniProt: A7ZVS7|DEOD_ECO24 Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)