Structure of PDB 4giu Chain B

Receptor sequence
>4giuB (length=346) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVG
IGFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAF
ADLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLT
FDPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGA
IVAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQ
3D structure
PDB4giu Repurposing the Chemical Scaffold of the Anti-Arthritic Drug Lobenzarit to Target Tryptophan Biosynthesis in Mycobacterium tuberculosis.
ChainB
Resolution1.667 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V106
Catalytic site (residue number reindexed from 1) V83
Enzyme Commision number 2.4.2.18: anthranilate phosphoribosyltransferase.
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 PRP B G107 G109 G110 N117 S119 T120 K135 N138 A140 S143 G146 G84 G86 G87 N94 S96 T97 K112 N115 A117 S120 G123
BS02 MG B S119 E252 S96 E229
BS03 MG B D251 E252 D228 E229
BS04 636 B N138 A179 H183 Y186 R193 G206 N115 A156 H160 Y163 R170 G183 MOAD: Ki=4.7uM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004048 anthranilate phosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4giu, PDBe:4giu, PDBj:4giu
PDBsum4giu
PubMed24623674
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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