Structure of PDB 1i80 Chain A

Receptor sequence
>1i80A (length=266) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DPRPDPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALGSPTTVL
PQAELPGFVPPTAAGHAGELLSVPIGAHRVLVLAGRIHAYEGHDLRYVVH
PVRAARAAGAQIMVLTNAAGGLRADLQVGQPVLISDHLNLTARSPLVGGE
FVDLTDAYSPRLRELARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGA
DLVGMSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEVLAAGAA
SATRMGALLADVIARF
3D structure
PDB1i80 Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucillin-H and its pieces.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S36 H68 H90 Y92 E93 A120 M207 S208 N231 A233 H243
Catalytic site (residue number reindexed from 1) S34 H66 H88 Y90 E91 A118 M205 S206 N229 A231 H241
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 PO4 A G35 S36 R88 H90 N119 A120 S208 G33 S34 R86 H88 N117 A118 S206
BS02 9HX A A120 A121 G122 E189 V205 G206 M207 N231 A118 A119 G120 E187 V203 G204 M205 N229 MOAD: Kd=0.39uM
BS03 IMR A S36 Y92 Y188 M207 H243 S34 Y90 Y186 M205 H241
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:0006154 adenosine catabolic process
GO:0006161 deoxyguanosine catabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1i80, PDBe:1i80, PDBj:1i80
PDBsum1i80
PubMed11444966
UniProtP9WP01|PUNA_MYCTU Purine nucleoside phosphorylase (Gene Name=punA)

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