Structure of PDB 1f52 Chain H Binding Site BS01
Receptor Information
>1f52 Chain H (length=468) [
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SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFD
GSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGY
DRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVA
IDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVME
QMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFG
KTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGG
VIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVAS
PKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDKNLYDLP
PEEAKEIPQVAGSLEEALNALDLDREFLKAGGVFTDEAIDAYIALRREED
DRVRMTPHPVEFELYYSV
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1f52 Chain H Residue 469 [
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Receptor-Ligand Complex Structure
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PDB
1f52
The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.
Resolution
2.49 Å
Binding residue
(original residue number in PDB)
E131 E212 E220
Binding residue
(residue number reindexed from 1)
E131 E212 E220
Annotation score
1
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:1f52
,
PDBe:1f52
,
PDBj:1f52
PDBsum
1f52
PubMed
11329256
UniProt
P0A1P6
|GLN1B_SALTY Glutamine synthetase (Gene Name=glnA)
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