Structure of PDB 1g2o Chain A

Receptor sequence
>1g2oA (length=262) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALGSPTTVLPQAE
LPGFVPPTAAGHAGELLSVPIGAHRVLVLAGRIHAYEGHDLRYVVHPVRA
ARAAGAQIMVLTNAAGGLRADLQVGQPVLISDHLNLTARSPLVGGEFVDL
TDAYSPRLRELARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVG
MSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEVLAAGAASATR
MGALLADVIARF
3D structure
PDB1g2o Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucillin-H and its pieces.
ChainA
Resolution1.75 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) S30 H62 H84 Y86 E87 A114 M201 S202 N225 A227 H237
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 S208 G29 S30 R82 H84 N113 S202
BS02 IMH A Y92 A120 G122 Y188 E189 V205 G206 M207 N231 H243 Y86 A114 G116 Y182 E183 V199 G200 M201 N225 H237 MOAD: Ki=28pM
PDBbind-CN: -logKd/Ki=10.55,Ki=28pM
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:1g2o, PDBe:1g2o, PDBj:1g2o
PDBsum1g2o
PubMed11444966
UniProtP9WP01|PUNA_MYCTU Purine nucleoside phosphorylase (Gene Name=punA)

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