Structure of PDB 8ooz Chain E

Receptor sequence
>8oozE (length=434) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSIEGSDMVLRPDPDTFRVLPWSGNEGTAEARLICDIELPDGKPFMGCP
RQVLKKNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYFDLA
PIDLAEEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALATADN
VITLKYVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNAFYD
PDAPDQISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPVYIT
WSGPNRSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDGVKN
KIEPPERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVSALG
EHVSQSIINVAMADWDSYRTQVHQWELDRYLQTY
3D structure
PDB8ooz Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
ChainE
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 E G129 E182 F197 K198 Y199 N245 S247 S327 R329 G121 E174 F189 K190 Y191 N237 S239 S319 R321
BS02 MG E E131 E331 E123 E323
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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