Structure of PDB 8oox Chain A Binding Site BS01
Receptor Information
>8oox Chain A (length=437) Species:
1122233
(Methermicoccus shengliensis DSM 18856) [
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SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSIEGFVRIEESDMVLRPDPDTFRVLPWSGTAEARLICDIELPDGKPFM
GCPRQVLKKNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYF
DLAPIDLAEEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALAT
ADNVITLKYVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNA
FYDPDAPDQISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPV
YITWSGPNRSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDG
VKNKIEPPERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVS
ALGEHVSQSIINVAMADWDSYRTQVHQWELDRYLQTY
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
8oox Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
8oox
Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
Resolution
3.09 Å
Binding residue
(original residue number in PDB)
E133 E187 E194
Binding residue
(residue number reindexed from 1)
E128 E182 E189
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8oox
,
PDBe:8oox
,
PDBj:8oox
PDBsum
8oox
PubMed
38243071
UniProt
A0A832VZP6
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