Structure of PDB 7tf9 Chain G

Receptor sequence
>7tf9G (length=443) Species: 1639 (Listeria monocytogenes) [Search protein sequence]
AKYTKEDIFRFADEQNVKFIRLQFTDILGIIKNVEIPVSQLKKALDNKIM
FDGSSIEGFVRIEESDMYLFPDLDTWVVFPWTAEKGKVARMICDIYNPDM
TPFAGDPRANLKRVLKEMEELGFTEFNLGPEPEFFLFKLDENRRPTLELN
DSGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
EDAITACDSIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHFNMSLF
NEKGNAFFDESGELELSQTAYHFLAGMLKHARGYTAVTNPTINSFKRLVP
GYEAPCYIAWSGKNRSPLVRVPSSRGLSTRLELRSVDPSANPYLAMAVLL
KAGLSGIKDELTPPAPVDRNIYGMNEEEREATGIYDLPESLGHALIELEK
NEIIKDGLGEHIFEHFIEAKTIECDMFRTAVHPWEREQYLEIY
3D structure
PDB7tf9 Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
ChainG
Resolution2.61 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
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 peptide G F60 V61 E419 M427 F59 V60 E418 M426
BS02 MG G E134 E189 E196 E133 E188 E195
BS03 MG G E132 H245 E333 E131 H244 E332
BS04 GLN G E134 Y156 E189 G241 G243 R298 E304 E133 Y155 E188 G240 G242 R297 E303
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7tf9, PDBe:7tf9, PDBj:7tf9
PDBsum7tf9
PubMed35778410
UniProtA0A5D5GA79

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