Structure of PDB 7tfc Chain I Binding Site BS04
Receptor Information
>7tfc Chain I (length=443) Species:
1423
(Bacillus subtilis) [
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AKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVM
FDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDG
TPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELN
DKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
AGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLF
KNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVP
GYEAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLL
AAGLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKS
NEVMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY
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
7tfc Chain I Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
7tfc
Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
Resolution
1.96 Å
Binding residue
(original residue number in PDB)
E134 E189 E196
Binding residue
(residue number reindexed from 1)
E133 E188 E195
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:7tfc
,
PDBe:7tfc
,
PDBj:7tfc
PDBsum
7tfc
PubMed
35778410
UniProt
A0A085CCI2
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