Structure of PDB 3of3 Chain B

Receptor sequence

>3of3B (length=240) Species: 666 (Vibrio cholerae)

ATPHINAQMGDFADVVLMPGDPLRAKYIAENFLDNAVQVCDVRNMFGYTG
TYKGRKISVMGHGMGIPSCSIYVTELIKDYGVKKIIRVGSCGAVNEGIKV
RDVVIGMGACTDSKVNRIRFKDHDFAAIADYKMVKAAEEAAKARGIDVKV
GNLFSAELFYTPDPSMFDVMDKYGIVGVEMEAAGIYGVAAEYGAKALAIC
TVSDHIKTGEQTTSEERQNTFNEMIEIALDSVLIGDQAGY

3D structure

• PDB: 3of3 Crystal structure of PNP with an inhibitor DADME_immH from Vibrio cholerae
• Chain: B
• Resolution: 1.83 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H18 G34 R38 R57 E89 R101 S104 S217 D218 I220 R231
• 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	DIH	B	M78 S104 C105 G106 F173 V192 E193 M194 E195 D218	M64 S90 C91 G92 F159 V178 E179 M180 E181 D204
BS02	DIH	B	H18 R57	H4 R43

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:0005829 cytosol

External links

• PDB: RCSB:3of3, PDBe:3of3, PDBj:3of3
• PDBsum: 3of3
• UniProt: Q9KPM0|DEOD1_VIBCH Purine nucleoside phosphorylase DeoD-type 1 (Gene Name=deoD1)