Structure of PDB 3uav Chain A

Receptor sequence
>3uavA (length=227) Species: 1396 (Bacillus cereus) [Search protein sequence]
SVHIEAKQGEIAESILLPGDPLRAKYIAETFLEDVTCYNNVRGMLGFTGT
YKGKRVSVQGTGMGVPSISIYVNELIQSYGVKNLIRVGTCGAIQKDVKVR
DVIIAMTACTDSNMNRLTFPGFDFAPAANFDLLKKAYDAGTEKGLHVRVG
NVLTADVFYRESMDMVKKLGDYGVLAVEMETTALYTLAAKYGVNALSVLT
VSDHIFSEERQTTFNEMIEIALDAAIQ
3D structure
PDB3uav Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H4 G20 R24 R43 E75 R87 T90 S203 D204 I206 R217
Catalytic site (residue number reindexed from 1) H3 G19 R23 R42 E74 R86 T89 S202 D203 I205 R210
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 SO4 A G20 R87 T90 G19 R86 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

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Cellular Component
External links
PDB RCSB:3uav, PDBe:3uav, PDBj:3uav
PDBsum3uav
PubMed22349225
UniProtQ5EEL8|DEOD_BACCE Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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