Structure of PDB 1vhw Chain E

Receptor sequence
>1vhwE (length=236) Species: 666 (Vibrio cholerae) [Search protein sequence]
TPHINAQMGDFADVVLMPGDPLRAKYIAENFLDNAVQVCDVRNMFGYTGT
YKGRRISVMGHGMGIPSCSIYVTELIKDYGVKKIIRVGSCGAVNEGIKVR
DVVIGMGACTDSKVNRIRFKDHDFAAIADYKMVKAAEEAAKARGIDVKVG
NLFSAELFYTPDPSMFDVMDKYGIVGVEMEAAGIYGVAAEYGAKALAICT
VSDHIKTGEQTTSEERQNTFNEMIEIALDSVLIGDQ
3D structure
PDB1vhw Structural analysis of a set of proteins resulting from a bacterial genomics project
ChainE
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H5 G21 R25 R44 E76 R88 S91 S204 D205 I207 R218
Catalytic site (residue number reindexed from 1) H3 G19 R23 R42 E74 R86 S89 S202 D203 I205 R216
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 ADN E H5 R44 H3 R42
BS02 ADN E M65 R88 S91 C92 F160 V179 M181 E182 M63 R86 S89 C90 F158 V177 M179 E180
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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Cellular Component
External links
PDB RCSB:1vhw, PDBe:1vhw, PDBj:1vhw
PDBsum1vhw
PubMed16021622
UniProtQ9KPM0|DEOD1_VIBCH Purine nucleoside phosphorylase DeoD-type 1 (Gene Name=deoD1)

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