Structure of PDB 5c7s Chain B

Receptor sequence

>5c7sB (length=343) Species: 83332 (Mycobacterium tuberculosis H37Rv)

SVPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMK
APTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMA
AIVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEV
GIGFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCA
FADLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKL
TFDPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAG
AIVAHAGLEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQ

3D structure

• PDB: 5c7s Binding and mimicking of the phosphate-rich substrate, PRPP
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V106
• Catalytic site (residue number reindexed from 1): V84
• 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	MN	B	D251 E252	D229 E230
BS02	MN	B	G107 S119 E252	G85 S97 E230
BS03	PRP	B	V106 G107 G110 N117 S119 T120 K135 N138 A141 S142 S143 G146	V84 G85 G88 N95 S97 T98 K113 N116 A119 S120 S121 G124

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:5c7s, PDBe:5c7s, PDBj:5c7s
• PDBsum: 5c7s
• UniProt: P9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)