Structure of PDB 3qqs Chain B

Receptor sequence
>3qqsB (length=346) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAAI
VVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGI
GFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFA
DLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTF
DPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAI
VAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
3D structure
PDB3qqs The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition.
ChainB
Resolution1.97 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) V82
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 V106 G109 N117 S119 T120 K135 A140 A141 S142 S143 G146 V82 G85 N93 S95 T96 K111 A116 A117 S118 S119 G122
BS02 MG B S119 E252 S95 E228
BS03 MG B D251 E252 D227 E228
BS04 17C B N138 P180 H183 Y186 R187 A190 R193 G206 N114 P156 H159 Y162 R163 A166 R169 G182
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:3qqs, PDBe:3qqs, PDBj:3qqs
PDBsum3qqs
PubMed23363292
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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