Structure of PDB 2bpq Chain B

Receptor sequence

>2bpqB (length=339) Species: 83332 (Mycobacterium tuberculosis H37Rv)

PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGGVNTVNLSTMAAIV
VAAAGVPVVKHGNRAAGGADTLEALGVRIDLGPDLVARSLAEVGIGFCFA
PRFHPSAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFADLAEVMAGV
FAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFDPAGFGFAR
AQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIVAHAGLSSA
EWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQILAA

3D structure

• PDB: 2bpq The Crystal Structure of Trpd, a Metabolic Enzyme Essential for Lung Colonization by Mycobacterium Tuberculosis, in Complex with its Substrate Phosphoribosylpyrophosphate
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V106
• Catalytic site (residue number reindexed from 1): V82
• 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	BEN	B	T70 M71 P74 V201 D225	T46 M47 P50 V168 D192
BS02	BEN	B	T353 A355	T319 A321

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:2bpq, PDBe:2bpq, PDBj:2bpq
• PDBsum: 2bpq
• PubMed: 16337227
• UniProt: P9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)