Structure of PDB 1f52 Chain D

Receptor sequence
>1f52D (length=468) [Search protein sequence]
SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGY
DRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVA
IDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVME
QMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFG
KTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGG
VIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVAS
PKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDKNLYDLP
PEEAKEIPQVAGSLEEALNALDLDREFLKAGGVFTDEAIDAYIALRREED
DRVRMTPHPVEFELYYSV
3D structure
PDB1f52 The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.
ChainD
Resolution2.49 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 D E131 E212 E220 E131 E212 E220
BS02 MN D E129 H269 E357 E129 H269 E357
BS03 ADP D G127 E129 E207 T223 R224 F225 H271 S273 R355 E357 G127 E129 E207 T223 R224 F225 H271 S273 R355 E357
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:1f52, PDBe:1f52, PDBj:1f52
PDBsum1f52
PubMed11329256
UniProtP0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)

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