Structure of PDB 8ooz Chain J

Receptor sequence
>8oozJ (length=431) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
GSKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHF
DGSSIEGSDMVLRPDPDTFRVLPWSTAEARLICDIELPDGKPFMGCPRQV
LKKNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYFDLAPID
LAEEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALATADNVIT
LKYVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNAFYDPDA
PDQISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPVYITWSG
PNRSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDGVKNKIE
PPERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVSALGEHV
SQSIINVAMADWDSYRTQVHQWELDRYLQTY
3D structure
PDB8ooz Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
ChainJ
Resolution2.7 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 ATP J G129 E182 K198 Y199 N245 S247 S327 R329 G118 E171 K187 Y188 N234 S236 S316 R318
BS02 MG J E131 H243 E331 E120 H232 E320
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:8ooz, PDBe:8ooz, PDBj:8ooz
PDBsum8ooz
PubMed38243071
UniProtA0A832VZP6

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