Structure of PDB 7tf9 Chain O Binding Site BS03

Receptor Information

>7tf9 Chain O (length=443) Species: 1639 (Listeria monocytogenes)

AKYTKEDIFRFADEQNVKFIRLQFTDILGIIKNVEIPVSQLKKALDNKIM
FDGSSIEGFVRIEESDMYLFPDLDTWVVFPWTAEKGKVARMICDIYNPDM
TPFAGDPRANLKRVLKEMEELGFTEFNLGPEPEFFLFKLDENRRPTLELN
DSGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
EDAITACDSIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHFNMSLF
NEKGNAFFDESGELELSQTAYHFLAGMLKHARGYTAVTNPTINSFKRLVP
GYEAPCYIAWSGKNRSPLVRVPSSRGLSTRLELRSVDPSANPYLAMAVLL
KAGLSGIKDELTPPAPVDRNIYGMNEEEREATGIYDLPESLGHALIELEK
NEIIKDGLGEHIFEHFIEAKTIECDMFRTAVHPWEREQYLEIY

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: 7tf9 Chain O Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7tf9 Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
• Resolution: 2.61 Å
• Binding residue (original residue number in PDB): E132 H245 E333
• Binding residue (residue number reindexed from 1): E131 H244 E332
• 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:7tf9, PDBe:7tf9, PDBj:7tf9
• PDBsum: 7tf9
• PubMed: 35778410
• UniProt: A0A5D5GA79