Structure of PDB 1lgr Chain J

Receptor sequence
>1lgrJ (length=445) [Search protein sequence]
SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRS
IAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEG
AWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVV
EAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFM
PKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAK
AINALANPTTNSYKRLVPPVMLAYSARNRSASIRIPVVASPKARRIEVRF
PDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDIPQVAGSLEEALNALDL
DREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
3D structure
PDB1lgr Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium.
ChainJ
Resolution2.79 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 MN J E131 E212 E220 E125 E206 E214
BS02 MN J E129 H269 E357 E123 H263 E347
BS03 AMP J E207 T223 F225 H271 S273 R355 E201 T217 F219 H265 S267 R345
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0019740 nitrogen utilization
GO:0051260 protein homooligomerization
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:1lgr, PDBe:1lgr, PDBj:1lgr
PDBsum1lgr
PubMed7727369
UniProtP0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)

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