Structure of PDB 1n3i Chain A

Receptor sequence
>1n3iA (length=262) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALGSPTTVLPQAE
LPGFVPPTAAGHAGELLSVPIGAHRVLVLAGRIHAYEGHDLRYVVHPVRA
ARAAGAQIMVLTNAAGGLRADLQVGQPVLISDHLNLTARSPLVGGEFVDL
TDAYSPRLRELARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVG
MSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEVLAAGAASATR
MGALLADVIARF
3D structure
PDB1n3i Over-The-Barrier Transition State Analogues Provide New Chemistries for Inhibitor Design: The Case of Purine Nucleoside Phosphorylase
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H68 H90 Y92 E93 A120 M207 S208 N231 A233 H243
Catalytic site (residue number reindexed from 1) H62 H84 Y86 E87 A114 M201 S202 N225 A227 H237
Enzyme Commision number 6.3.2.1: pantoate--beta-alanine ligase (AMP-forming).
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 DIH A Y92 A120 A121 G122 Y188 E189 V205 M207 N231 H243 Y86 A114 A115 G116 Y182 E183 V199 M201 N225 H237 MOAD: Kd=1.3nM
PDBbind-CN: -logKd/Ki=8.89,Ki=1.3nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016763 pentosyltransferase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0009116 nucleoside metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1n3i, PDBe:1n3i, PDBj:1n3i
PDBsum1n3i
PubMed12755607
UniProtP9WIL5|PANC_MYCTU Pantothenate synthetase (Gene Name=panC)

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