Structure of PDB 8ooz Chain H

Receptor sequence
>8oozH (length=428) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence]
SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSISDMVLRPDPDTFRVLPWSTAEARLICDIELPDGKPFMGCPRQVLKK
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.
ChainH
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 H G129 E182 F197 K198 Y199 N245 S247 R329 G115 E168 F183 K184 Y185 N231 S233 R315
BS02 MG H 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

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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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