Structure of PDB 8ooz Chain C

Receptor sequence
>8oozC (length=428) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
GSKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHF
DGSSIEDMVLRPDPDTFRVLPWTAEARLICDIELPDGKPFMGCPRQVLKK
NMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYFDLAPIDLAE
EIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALATADNVITLKY
VAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNAFYDPDAPDQ
ISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPVYITWSGPNR
SSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDGVKNKIEPPE
RVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVSALGEHVSQS
IINVAMADWDSYRTQVHQWELDRYLQTY
3D structure
PDB8ooz Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
ChainC
Resolution2.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C E182 F197 K198 Y199 N245 S247 S327 R329 E168 F183 K184 Y185 N231 S233 S313 R315
BS02 MG C E133 E187 E194 E119 E173 E180
BS03 MG C E131 H243 E331 E117 H229 E317
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8ooz, PDBe:8ooz, PDBj:8ooz
PDBsum8ooz
PubMed38243071
UniProtA0A832VZP6

[Back to BioLiP]