Structure of PDB 4owu Chain A

Receptor sequence

>4owuA (length=347) Species: 1773 (Mycobacterium tuberculosis)

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVG
IGFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAF
ADLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLT
FDPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGA
IVAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI

3D structure

• PDB: 4owu Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
• Chain: A
• 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	A	D251 E252	D228 E229
BS02	MG	A	S119 E252	S96 E229
BS03	PRP	A	G107 G109 G110 N117 S119 T120 K135 A141 S143 G146	G84 G86 G87 N94 S96 T97 K112 A118 S120 G123
BS04	5M0	A	N138 P180 Y186 R187 A190	N115 P157 Y163 R164 A167

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