Structure of PDB 3qs8 Chain D

Receptor sequence
>3qs8D (length=346) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAAI
VVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGI
GFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFA
DLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTF
DPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAI
VAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
3D structure
PDB3qs8 The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition.
ChainD
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) 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 D G107 G109 G110 N117 S119 T120 K135 A140 A141 S143 G146 G83 G85 G86 N93 S95 T96 K111 A116 A117 S119 G122
BS02 MG D S119 E252 S95 E228
BS03 MG D D251 E252 D227 E228
BS04 17D D M86 G107 N138 A179 Y186 R193 G206 M62 G83 N114 A155 Y162 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:3qs8, PDBe:3qs8, PDBj:3qs8
PDBsum3qs8
PubMed23363292
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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