Structure of PDB 1pr1 Chain A

Receptor sequence

>1pr1A (length=226) Species: 562 (Escherichia coli)

ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHRQTTFNDMIKIALESVLLGDK

3D structure

• PDB: 1pr1 Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H4 G20 R24 R43 E75 R87 S90 S203 D204 R217
• Catalytic site (residue number reindexed from 1): H4 G20 R24 R43 E75 R87 S90 S203 D204 R206
• 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	R87 G89 S90	R87 G89 S90
BS02	FMB	A	M64 R87 S90 C91 G92 F159 V178 M180 E181 D204	M64 R87 S90 C91 G92 F159 V178 M180 E181 D204	MOAD: Ki=5uM PDBbind-CN: -logKd/Ki=5.30,Ki=5uM

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:1pr1, PDBe:1pr1, PDBj:1pr1
• PDBsum: 1pr1
• PubMed: 12937174
• UniProt: P0ABP9|DEOD_ECO57 Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)