Structure of PDB 4x5c Chain B

Receptor sequence

>4x5cB (length=345) Species: 1773 (Mycobacterium tuberculosis)

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGTVNLSTMAAIV
VAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGIG
FCFAPRFHPSYRHAAAVLREIGVPTVFNLLGPLTNPARPRAGLIGCAFAD
LAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFD
PAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIV
AHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI

3D structure

• PDB: 4x5c Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.
• Chain: B
• Resolution: 2.33 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	POP	B	G107 N117 S119 T120 G146	G84 N92 S94 T95 G121
BS02	MG	B	G107 S119 E252	G84 S94 E227
BS03	MG	B	D251 E252	D226 E227

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:4x5c, PDBe:4x5c, PDBj:4x5c
• PDBsum: 4x5c
• PubMed: 26356348
• UniProt: P9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)