Structure of PDB 4own Chain A Binding Site BS04

Receptor Information
>4own Chain A (length=344) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRALSGGADTLEALGVRIDLGPDLVARSLAEVGIGF
CFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFADL
AEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFDP
AGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIVA
HAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
Ligand information
Ligand ID5RG
InChIInChI=1S/C7H6FNO2/c8-4-1-2-6(9)5(3-4)7(10)11/h1-3H,9H2,(H,10,11)
InChIKeyFPQMGQZTBWIHDN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.2c1cc(c(cc1F)C(=O)O)N
CACTVS 3.370Nc1ccc(F)cc1C(O)=O
ACDLabs 12.01O=C(O)c1cc(F)ccc1N
FormulaC7 H6 F N O2
Name2-amino-5-fluorobenzoic acid
ChEMBLCHEMBL4585642
DrugBank
ZINCZINC000000165667
PDB chain4own Chain A Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4own Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
Resolution2.11 Å
Binding residue
(original residue number in PDB)		V106 G107 H136 G137 N138 G206
Binding residue
(residue number reindexed from 1)		V83 G84 H113 G114 N115 G180
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=4.22,Ki=60uM
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.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4own, PDBe:4own, PDBj:4own
PDBsum4own
PubMed24712732
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

[Back to BioLiP]