Structure of PDB 8oow Chain H

Receptor sequence
>8oowH (length=430) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSIESDMVLRPDPDTFRVLPWSGTAEARLICDIELPDGKPFMGCPRQVL
KKNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYFDLAPIDL
AEEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALATADNVITL
KYVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNAFYDPDAP
DQISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPVYITWSGP
NRSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDGVKNKIEP
PERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVSALGEHVS
QSIINVAMADWDSYRTQVHQWELDRYLQTY
3D structure
PDB8oow Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
ChainH
Resolution2.64 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 H H243 E331 R333 H231 E319 R321
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:8oow, PDBe:8oow, PDBj:8oow
PDBsum8oow
PubMed38243071
UniProtA0A832VZP6

[Back to BioLiP]