Structure of PDB 7tfb Chain T

Receptor sequence
>7tfbT (length=441) Species: 1406 (Paenibacillus polymyxa) [Search protein sequence]
SYTREDIIRIAEEENVRFIRLQFTDLLGTIKNVEIPVSQLEKALDNKMMF
DGSSIEGYVRIEESDMYLYPDLDTWVVFPWVTSDRVARLICDIYKPDGSP
FAGDPRGILKRVLKEAEELGYTSMNVGPEPEFFLFKTDEKGDPTTELNDQ
GGYFDLAPMDLGENCRREIVLKLEEMGFEIEASHHEVAPGQHEIDFKYAD
AVKAADQIQTFKLVVKTIARQHGLHATFMPKPLFGVNGSGMHCNQSLFKD
NENVFYDETDELGLSQTARHYMAGILKHARAMAAITNPTVNSYKRLVPGY
EAPCYVAWSASNRSPMIRIPASRGLSTRVEVRNPDPAANPYLALAVMLRA
GLDGIKRQMALPAPIDRNIYVMSEEERIEEGIPSLPADLKEALSELIRSE
VISDALGDHALAYFYELKEIEWDMYRTQVHQWERDQYLTLY
3D structure
PDB7tfb Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
ChainT
Resolution2.28 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 Y59 R61 M425 Y58 R60 M424
BS02 peptide T G300 Y301 R314 G299 Y300 R313
BS03 MG T E132 E187 E194 E131 E186 E193
BS04 MG T E130 H243 E331 E129 H242 E330
BS05 GLN T E132 Y154 E187 G239 G241 R296 E302 E131 Y153 E186 G238 G240 R295 E301
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:7tfb, PDBe:7tfb, PDBj:7tfb
PDBsum7tfb
PubMed35778410
UniProtA0A0F0G8G2

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