Structure of PDB 7tf6 Chain T

Receptor sequence
>7tf6T (length=438) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TFTKEDIRKFAEEENVRYLRLQFTDILGTIKNVEVPVSQLEKVLDNEMMF
DGSSIEGFVRIEESDMYLHPDLDTWVIFPWGKVARLICDVYKTDGTPFEG
DPRANLKRVLKEMEDLGFTDFNLGPEPEFFLFKLDEKGEPTLELNDDGGY
FDLAPTDLGENCRRDIVLELEDMGFDIEASHHEVAPGQHEIDFKYADAVT
ACDNIQTFKLVVKTIARKHNLHATFMPKPLFGVNGSGMHFNVSLFKGKEN
AFFDPNTEMGLTETAYQFTAGVLKNARGFTAVCNPLVNSYKRLVPGYEAP
CYIAWSGKNRSPLIRVPSSRGLSTRIEVRSVDPAANPYMALAAILEAGLD
GIKNKLKVPEPVNQNIYEMNREEREAVGIQDLPSTLYTALKAMRENEVIK
KALGNHIYNQFINSKSIEWDYYRTQVSEWERDQYMKQY
3D structure
PDB7tf6 Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
ChainT
Resolution2.15 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 T F62 R64 I65 Y429 F58 R60 I61 Y421
BS02 peptide T G240 N242 G304 Y305 R318 Y375 G232 N234 G296 Y297 R310 Y367
BS03 peptide T Q441 Q445 Q433 Q437
BS04 MG T E136 E191 E198 E128 E183 E190
BS05 MG T E134 H247 E335 E126 H239 E327
BS06 GLN T E136 E191 G243 H247 R300 E306 E128 E183 G235 H239 R292 E298
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:7tf6, PDBe:7tf6, PDBj:7tf6
PDBsum7tf6
PubMed35778410
UniProtE3VXC2

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