Structure of PDB 1pr0 Chain A

Receptor sequence

>1pr0A (length=237) Species: 83334 (Escherichia coli O157:H7)

ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK

3D structure

• PDB: 1pr0 Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase.
• Chain: A
• Resolution: 2.2 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	PO4	A	G20 R87 G89 S90	G20 R87 G89 S90
BS02	NOS	A	R87 S90 C91 F159 V178 E179 M180 E181 D204	R87 S90 C91 F159 V178 E179 M180 E181 D204

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:1pr0, PDBe:1pr0, PDBj:1pr0
• PDBsum: 1pr0
• PubMed: 12937174
• UniProt: P0ABP9|DEOD_ECO57 Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)