Structure of PDB 7tfb Chain b Binding Site BS02

Receptor Information
>7tfb Chain b (length=441) Species: 1406 (Paenibacillus polymyxa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SYTREDIIRIAEEENVRFIRLQFTDLLGTIKNVEIPVSQLEKALDNKMMF
DGSSIEGYVRIEESDMYLYPDLDTWVVFPWVTSDRVARLICDIYKPDGSP
FAGDPRGILKRVLKEAEELGYTSMNVGPEPEFFLFKTDEKGDPTTELNDQ
GGYFDLAPMDLGENCRREIVLKLEEMGFEIEASHHEVAPGQHEIDFKYAD
AVKAADQIQTFKLVVKTIARQHGLHATFMPKPLFGVNGSGMHCNQSLFKD
NENVFYDETDELGLSQTARHYMAGILKHARAMAAITNPTVNSYKRLVPGY
EAPCYVAWSASNRSPMIRIPASRGLSTRVEVRNPDPAANPYLALAVMLRA
GLDGIKRQMALPAPIDRNIYVMSEEERIEEGIPSLPADLKEALSELIRSE
VISDALGDHALAYFYELKEIEWDMYRTQVHQWERDQYLTLY
Ligand information
>7tfb Chain a (length=10) Species: 1406 (Paenibacillus polymyxa) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
LIQGELSRFF
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB7tfb Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
Resolution2.28 Å
Binding residue
(original residue number in PDB)
N238 Y301 R314
Binding residue
(residue number reindexed from 1)
N237 Y300 R313
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7tfb, PDBe:7tfb, PDBj:7tfb
PDBsum7tfb
PubMed35778410
UniProtA0A0F0G8G2

[Back to BioLiP]