Structure of PDB 7tfa Chain T Binding Site BS03

Receptor Information

>7tfa Chain T (length=441) Species: 1406 (Paenibacillus polymyxa)

SYTREDIIRIAEEENVRFIRLQFTDLLGTIKNVEIPVSQLEKALDNKMMF
DGSSIEGYVRIEESDMYLYPDLDTWVVFPWVTSDRVARLICDIYKPDGSP
FAGDPRGILKRVLKEAEELGYTSMNVGPEPEFFLFKTDEKGDPTTELNDQ
GGYFDLAPMDLGENCRREIVLKLEEMGFEIEASHHEVAPGQHEIDFKYAD
AVKAADQIQTFKLVVKTIARQHGLHATFMPKPLFGVNGSGMHCNQSLFKD
NENVFYDETDELGLSQTARHYMAGILKHARAMAAITNPTVNSYKRLVPGY
EAPCYVAWSASNRSPMIRIPASRGLSTRVEVRNPDPAANPYLALAVMLRA
GLDGIKRQMALPAPIDRNIYVMSEEERIEEGIPSLPADLKEALSELIRSE
VISDALGDHALAYFYELKEIEWDMYRTQVHQWERDQYLTLY

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: 7tfa Chain T Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7tfa Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
• Resolution: 2.07 Å
• Binding residue (original residue number in PDB): E132 E187 E194
• Binding residue (residue number reindexed from 1): E131 E186 E193
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 6.3.1.2: glutamine synthetase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004356 glutamine synthetase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006542 glutamine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:7tfa, PDBe:7tfa, PDBj:7tfa
• PDBsum: 7tfa
• PubMed: 35778410
• UniProt: A0A0F0G8G2