Structure of PDB 4s0r Chain B

Receptor sequence

>4s0rB (length=443) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]

AKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVM
FDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDG
TPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELN
DKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
AGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLF
KNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVP
GYEAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLL
AAGLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKS
NEVMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY

3D structure

PDB

4s0r Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis.

Chain

Resolution

3.5 Å

3D
structure

Catalytic site residues are labeled in the structure
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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)
BS01	peptide	B	F60 R62 M427	F59 R61 M426
BS02	peptide	B	Q439 Q443	Q438 Q442
BS03	peptide	B	K153 D158 A191 P192 G238 V239 N240 P301 G302 Y303 Y308 R316 Y373	K152 D157 A190 P191 G237 V238 N239 P300 G301 Y302 Y307 R315 Y372
BS04	GLN	B	E134 E189 V190 Q194 N240 H245 E304	E133 E188 V189 Q193 N239 H244 E303
BS05	MG	B	E134 E196 H245	E133 E195 H244
BS06	MG	B	H245 E333	H244 E332

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

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:4s0r, PDBe:4s0r, PDBj:4s0r
PDBsum	4s0r
PubMed	25691471
UniProt	P12425\|GLN1A_BACSU Glutamine synthetase (Gene Name=glnA)

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