Structure of PDB 7tfb Chain D Binding Site BS04
Receptor Information
>7tfb Chain D (length=441) Species:
1406
(Paenibacillus polymyxa) [
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SYTREDIIRIAEEENVRFIRLQFTDLLGTIKNVEIPVSQLEKALDNKMMF
DGSSIEGYVRIEESDMYLYPDLDTWVVFPWVTSDRVARLICDIYKPDGSP
FAGDPRGILKRVLKEAEELGYTSMNVGPEPEFFLFKTDEKGDPTTELNDQ
GGYFDLAPMDLGENCRREIVLKLEEMGFEIEASHHEVAPGQHEIDFKYAD
AVKAADQIQTFKLVVKTIARQHGLHATFMPKPLFGVNGSGMHCNQSLFKD
NENVFYDETDELGLSQTARHYMAGILKHARAMAAITNPTVNSYKRLVPGY
EAPCYVAWSASNRSPMIRIPASRGLSTRVEVRNPDPAANPYLALAVMLRA
GLDGIKRQMALPAPIDRNIYVMSEEERIEEGIPSLPADLKEALSELIRSE
VISDALGDHALAYFYELKEIEWDMYRTQVHQWERDQYLTLY
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
7tfb Chain D Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
7tfb
Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
Resolution
2.28 Å
Binding residue
(original residue number in PDB)
E130 H243 E331
Binding residue
(residue number reindexed from 1)
E129 H242 E330
Annotation score
1
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
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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
PDBsum
7tfb
PubMed
35778410
UniProt
A0A0F0G8G2
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