Structure of PDB 8oox Chain A

Receptor sequence
>8ooxA (length=437) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSIEGFVRIEESDMVLRPDPDTFRVLPWSGTAEARLICDIELPDGKPFM
GCPRQVLKKNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYF
DLAPIDLAEEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALAT
ADNVITLKYVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNA
FYDPDAPDQISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPV
YITWSGPNRSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDG
VKNKIEPPERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVS
ALGEHVSQSIINVAMADWDSYRTQVHQWELDRYLQTY
3D structure
PDB8oox Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
ChainA
Resolution3.09 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 MG A E133 E187 E194 E128 E182 E189
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:8oox, PDBe:8oox, PDBj:8oox
PDBsum8oox
PubMed38243071
UniProtA0A832VZP6

[Back to BioLiP]