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Structure of PDB 1fpy Chain C Binding Site BS04

Receptor Information
>1fpy Chain C (length=468) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGY
DRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVA
IDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVME
QMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFG
KTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGG
VIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVAS
PKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDKNLYDLP
PEEAKEIPQVAGSLEEALNALDLDREFLKAGGVFTDEAIDAYIALRREED
DRVRMTPHPVEFELYYSV
Ligand information
Ligand IDPPQ
InChIInChI=1S/C5H12NO4P/c1-11(9,10)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)(H,9,10)/t4-/m0/s1
InChIKeyIAJOBQBIJHVGMQ-BYPYZUCNSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[P@](O)(=O)CC[C@H](N)C(O)=O
ACDLabs 10.04O=P(O)(C)CCC(C(=O)O)N
OpenEye OEToolkits 1.5.0CP(=O)(CCC(C(=O)O)N)O
OpenEye OEToolkits 1.5.0C[P@](=O)(CC[C@@H](C(=O)O)N)O
CACTVS 3.341C[P](O)(=O)CC[CH](N)C(O)=O
FormulaC5 H12 N O4 P
NamePHOSPHINOTHRICIN;
2-AMINO-4-(HYDROXYMETHYL-PHOSPHINYL)BUTANOIC ACID
ChEMBLCHEMBL145114
DrugBank
ZINCZINC000000902209
PDB chain1fpy Chain C Residue 5902 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1fpy The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.
Resolution2.89 Å
Binding residue
(original residue number in PDB)		E131 E212 G265 H269 R321 E327 R359
Binding residue
(residue number reindexed from 1)		E131 E212 G265 H269 R321 E327 R359
Annotation score2
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
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Cellular Component
External links
PDB RCSB:1fpy, PDBe:1fpy, PDBj:1fpy
PDBsum1fpy
PubMed11329256
UniProtP0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)

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