Structure of PDB 5byt Chain B Binding Site BS01

Receptor Information

>5byt Chain B (length=343) Species: 83332 (Mycobacterium tuberculosis H37Rv)

VPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKA
PTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAA
IVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVG
IGFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAF
ADLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLT
FDPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGA
IVAHAGLSEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQ

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5byt Chain B Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5byt Binding and mimicking of the phosphate-rich substrate, PRPP.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): S119 E252
• Binding residue (residue number reindexed from 1): S96 E229
• Annotation score: 1

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

External links

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