Structure of PDB 3uay Chain A

Receptor sequence

>3uayA (length=233) Species: 1396 (Bacillus cereus)

SVHIEAKQGEIAESILLPGDPLRAKYIAETFLEDVTCYNNVRGMLGFTGT
YKGKRVSVQGTGMGVPSISIYVNELIQSYGVKNLIRVGTCGAIQKDVKVR
DVIIAMTACTDSNMNRLTFPGFDFAPAANFDLLKKAYDAGTEKGLHVRVG
NVLTADVFYRESMDMVKKLGDYGVLAVEMETTALYTLAAKYGVNALSVLT
VSNHIFTGEETTSEERQTTFNEMIEIALDAAIQ

3D structure

• PDB: 3uay Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase.
• Chain: A
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H4 G20 R24 R43 E75 R87 T90 S203 N204 I206 R217
• Catalytic site (residue number reindexed from 1): H3 G19 R23 R42 E74 R86 T89 S202 N203 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	A	M64 T90 C91 F159 E179 M180 E181 N204 I206	M63 T89 C90 F158 E178 M179 E180 N203 I205
BS02	SO4	A	G20 R87 G89 T90	G19 R86 G88 T89

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:3uay, PDBe:3uay, PDBj:3uay
• PDBsum: 3uay
• PubMed: 22349225
• UniProt: Q5EEL8|DEOD_BACCE Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)