Structure of PDB 1fpy Chain K

Receptor sequence

>1fpyK (length=468)

SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGY
DRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVA
IDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVME
QMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFG
KTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGG
VIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVAS
PKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDKNLYDLP
PEEAKEIPQVAGSLEEALNALDLDREFLKAGGVFTDEAIDAYIALRREED
DRVRMTPHPVEFELYYSV

3D structure

• PDB: 1fpy The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.
• Chain: K
• Resolution: 2.89 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	K	E131 E212 E220	E131 E212 E220
BS02	MN	K	E129 H269 E357	E129 H269 E357
BS03	ADP	K	G127 E129 E207 T223 F225 H271 S273 R355 E357	G127 E129 E207 T223 F225 H271 S273 R355 E357
BS04	PPQ	K	E131 E212 G265 H269 R321 E327 R359	E131 E212 G265 H269 R321 E327 R359

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:1fpy, PDBe:1fpy, PDBj:1fpy
• PDBsum: 1fpy
• PubMed: 11329256
• UniProt: P0A1P6|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)