Structure of PDB 2lgs Chain G

Receptor sequence

>2lgsG (length=445)

SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRS
IAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEG
AWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVV
EAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFM
PKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAK
AINALANPTTNSYKRLVPPVMLAYSARNRSASIRIPVVASPKARRIEVRF
PDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDIPQVAGSLEEALNALDL
DREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV

3D structure

• PDB: 2lgs Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine.
• Chain: G
• Resolution: 2.8 Å

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	G	E131 E212 E220	E125 E206 E214
BS02	MN	G	E129 H269 E357	E123 H263 E347
BS03	GLU	G	E131 N264 G265 G267 H269 R321 R359	E125 N258 G259 G261 H263 R315 R349

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

External links

• PDB: RCSB:2lgs, PDBe:2lgs, PDBj:2lgs
• PDBsum: 2lgs
• PubMed: 8099447
• UniProt: P0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)