Structure of PDB 2lgs Chain E Binding Site BS03

Receptor Information
>2lgs Chain E (length=445) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRS
IAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEG
AWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVV
EAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFM
PKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAK
AINALANPTTNSYKRLVPPVMLAYSARNRSASIRIPVVASPKARRIEVRF
PDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDIPQVAGSLEEALNALDL
DREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
Ligand information
Ligand IDGLU
InChIInChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1
InChIKeyWHUUTDBJXJRKMK-VKHMYHEASA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)C(N)CCC(=O)O
OpenEye OEToolkits 1.7.0C(CC(=O)O)C(C(=O)O)N
OpenEye OEToolkits 1.7.0C(CC(=O)O)[C@@H](C(=O)O)N
CACTVS 3.370N[C@@H](CCC(O)=O)C(O)=O
CACTVS 3.370N[CH](CCC(O)=O)C(O)=O
FormulaC5 H9 N O4
NameGLUTAMIC ACID
ChEMBLCHEMBL575060
DrugBankDB00142
ZINCZINC000001482113
PDB chain2lgs Chain E Residue 471 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2lgs Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		E131 N264 G265 G267 H269 R321 R359
Binding residue
(residue number reindexed from 1)		E125 N258 G259 G261 H263 R315 R349
Annotation score5
Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
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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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2lgs, PDBe:2lgs, PDBj:2lgs
PDBsum2lgs
PubMed8099447
UniProtP0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)

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