Structure of PDB 4s0r Chain G

Receptor sequence
>4s0rG (length=443) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
AKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVM
FDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDG
TPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELN
DKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
AGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLF
KNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVP
GYEAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLL
AAGLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKS
NEVMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY
3D structure
PDB4s0r Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis.
ChainG
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D53 E132 E134 E189 E196 H245 R316 E333 R335
Catalytic site (residue number reindexed from 1) D52 E131 E133 E188 E195 H244 R315 E332 R334
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 peptide G F60 R62 M427 F59 R61 M426
BS02 peptide G A191 G238 V239 N240 P301 G302 Y303 Y308 R316 R370 Y373 R380 A190 G237 V238 N239 P300 G301 Y302 Y307 R315 R369 Y372 R379
BS03 GLN G E134 Y156 E189 E304 E133 Y155 E188 E303
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016595 glutamate binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
GO:0070406 glutamine binding
GO:0140297 DNA-binding transcription factor binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0043562 cellular response to nitrogen levels
GO:0045892 negative regulation of DNA-templated transcription
GO:0090295 nitrogen catabolite repression of transcription
GO:1904797 negative regulation of core promoter binding
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4s0r, PDBe:4s0r, PDBj:4s0r
PDBsum4s0r
PubMed25691471
UniProtP12425|GLN1A_BACSU Glutamine synthetase (Gene Name=glnA)

[Back to BioLiP]