Structure of PDB 4owq Chain B

Receptor sequence

>4owqB (length=345) Species: 1773 (Mycobacterium tuberculosis)

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRALSGGADTLEALGVRIDLGPDLVARSLAEVGIGF
CFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFADL
AEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFDP
AGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIVA
HAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQIL

3D structure

• PDB: 4owq Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
• Chain: B
• Resolution: 1.89 Å

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	MG	B	S119 E252	S96 E226
BS02	PRP	B	G110 N117 S119 T120 K135	G87 N94 S96 T97 K112
BS03	3M0	B	P180 H183 Y186 A190 R194	P154 H157 Y160 A164 R168

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

External links

• PDB: RCSB:4owq, PDBe:4owq, PDBj:4owq
• PDBsum: 4owq
• PubMed: 24712732
• UniProt: P9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)