Structure of PDB 4own Chain B

Receptor sequence

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

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAASLSGGADTLEALGVRIDLGPDLVARSLAEVGI
GFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFA
DLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTF
DPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAI
VAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQIL

3D structure

• PDB: 4own Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
• Chain: B
• Resolution: 2.11 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 E228
BS02	MG	B	D251 E252	D227 E228
BS03	PRP	B	G109 G110 N117 S119 T120 K135	G86 G87 N94 S96 T97 K112
BS04	5RG	B	N138 P180 H183 Y186 R187 A190	N115 P156 H159 Y162 R163 A166
BS05	5RG	B	V106 G107 H136 N138 G206	V83 G84 H113 N115 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

External links

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