Structure of PDB 4owm Chain B

Receptor sequence

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

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAALSGGADTLEALGVRIDLGPDLVARSLAEVGIG
FCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFAD
LAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFD
PAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIV
AHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQILE

3D structure

• PDB: 4owm Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
• Chain: B
• Resolution: 1.99 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 E227
BS02	MG	B	D251 E252	D226 E227
BS03	PRP	B	G107 G109 G110 N117 S119 T120 K135 A140 A141 G146	G84 G86 G87 N94 S96 T97 K112 A117 A118 G121
BS04	3F0	B	P180 H183 Y186 A190	P155 H158 Y161 A165

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