Structure of PDB 3of3 Chain C

Receptor sequence
>3of3C (length=240) Species: 666 (Vibrio cholerae) [Search protein sequence]
ATPHINAQMGDFADVVLMPGDPLRAKYIAENFLDNAVQVCDVRNMFGYTG
TYKGRKISVMGHGMGIPSCSIYVTELIKDYGVKKIIRVGSCGAVNEGIKV
RDVVIGMGACTDSKVNRIRFKDHDFAAIADYKMVKAAEEAAKARGIDVKV
GNLFSAELFYTPDPSMFDVMDKYGIVGVEMEAAGIYGVAAEYGAKALAIC
TVSDHIKTGEQTTSEERQNTFNEMIEIALDSVLIGDQAGY
3D structure
PDB3of3 Crystal structure of PNP with an inhibitor DADME_immH from Vibrio cholerae
ChainC
Resolution1.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C M78 S104 C105 F173 V192 E193 M194 E195 D218 M64 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:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:3of3, PDBe:3of3, PDBj:3of3
PDBsum3of3
PubMed
UniProtQ9KPM0|DEOD1_VIBCH Purine nucleoside phosphorylase DeoD-type 1 (Gene Name=deoD1)

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