Structure of PDB 1vhw Chain D

Receptor sequence

>1vhwD (length=237) Species: 666 (Vibrio cholerae)

ATPHINAQMGDFADVVLMPGDPLRAKYIAENFLDNAVQVCDVRNMFGYTG
TYKGRRISVMGHGMGIPSCSIYVTELIKDYGVKKIIRVGSCGAVNEGIKV
RDVVIGMGACTDSKVNRIRFKDHDFAAIADYKMVKAAEEAAKARGIDVKV
GNLFSAELFYTPDPSMFDVMDKYGIVGVEMEAAGIYGVAAEYGAKALAIC
TVSDHIKTGEQTTSEERQNTFNEMIEIALDSVLIGDQ

3D structure

• PDB: 1vhw Structural analysis of a set of proteins resulting from a bacterial genomics project
• Chain: D
• Resolution: 1.54 Å

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): 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	ADN	D	H5 R44	H4 R43
BS02	ADN	D	M65 R88 S91 C92 F160 V179 M181 E182	M64 R87 S90 C91 F159 V178 M180 E181

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:1vhw, PDBe:1vhw, PDBj:1vhw
• PDBsum: 1vhw
• PubMed: 16021622
• UniProt: Q9KPM0|DEOD1_VIBCH Purine nucleoside phosphorylase DeoD-type 1 (Gene Name=deoD1)