Structure of PDB 7tfc Chain P

Receptor sequence
>7tfcP (length=443) Species: 1423 (Bacillus subtilis) [Search protein sequence]
AKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVM
FDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDG
TPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELN
DKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
AGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLF
KNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVP
GYEAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLL
AAGLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKS
NEVMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY
3D structure
PDB7tfc Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
ChainP
Resolution1.96 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 P Q439 Q443 Q438 Q442
BS02 peptide P F60 R62 I63 E424 M427 F59 R61 I62 E423 M426
BS03 peptide P G302 R316 N371 G301 R315 N370
BS04 MG P E134 E189 E196 E133 E188 E195
BS05 MG P E132 H245 E333 E131 H244 E332
BS06 GLN P Y156 E189 G241 H245 R298 E304 Y155 E188 G240 H244 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:7tfc, PDBe:7tfc, PDBj:7tfc
PDBsum7tfc
PubMed35778410
UniProtA0A085CCI2

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