Structure of PDB 4x59 Chain B

Receptor sequence
>4x59B (length=347) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVG
IGFCFAARFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAF
ADLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLT
FDPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGA
IVAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
3D structure
PDB4x59 Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.
ChainB
Resolution1.8 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 V106 G107 T108 N117 S119 T120 K135 A141 G146 V83 G84 T85 N94 S96 T97 K112 A118 G123
BS02 MG B S119 E252 S96 E229
BS03 MG B D251 E252 D228 E229
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:4x59, PDBe:4x59, PDBj:4x59
PDBsum4x59
PubMed26356348
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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