Structure of PDB 7tno Chain D Binding Site BS02

Receptor Information

>7tno Chain D (length=600) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLT
IVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSK
PFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLV
SRFSPQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWF
FTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKE
FFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLEST
MNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQG
VLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAM
LVALIEFCYKSRLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVC
KTKVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRA
SSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGI
IVYISANAGKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLTG

Ligand information

Ligand ID

CYZ

InChI

InChI=1S/C14H16ClN3O4S2/c15-10-5-11-13(6-12(10)23(16,19)20)24(21,22)18-14(17-11)9-4-7-1-2-8(9)3-7/h1-2,5-9,14,17-18H,3-4H2,(H2,16,19,20)/t7-,8+,9-,14-/m0/s1

InChIKey

BOCUKUHCLICSIY-KSCJFIISSA-N

SMILES

Software	SMILES
ACDLabs 10.04	O=S(=O)(c1c(Cl)cc2c(c1)S(=O)(=O)NC(N2)C4C3C=CC(C3)C4)N
CACTVS 3.341	N[S](=O)(=O)c1cc2c(N[C@@H](N[S]2(=O)=O)[C@H]3C[C@@H]4C[C@H]3C=C4)cc1Cl
CACTVS 3.341	N[S](=O)(=O)c1cc2c(N[CH](N[S]2(=O)=O)[CH]3C[CH]4C[CH]3C=C4)cc1Cl
OpenEye OEToolkits 1.5.0	c1c2c(cc(c1Cl)S(=O)(=O)N)S(=O)(=O)NC(N2)C3CC4CC3C=C4
OpenEye OEToolkits 1.5.0	c1c2c(cc(c1Cl)S(=O)(=O)N)S(=O)(=O)N[C@H](N2)[C@H]3C[C@@H]4C[C@H]3C=C4

Formula

C14 H16 Cl N3 O4 S2

Name

CYCLOTHIAZIDE;
3-BICYCLO[2.2.1]HEPT-5-EN-2-YL-6-CHLORO-3,4- DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE-7-SULFONAMIDE 1,1 DIOXIDE

PDB chain

7tno Chain D Residue 1301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	7tno Opening of glutamate receptor channel to subconductance levels.
Resolution	4.02 Å
Binding residue (original residue number in PDB)	P494 F495 M496 S497 L751 S754 L759 D760 K763
Binding residue (residue number reindexed from 1)	P101 F102 M103 S104 L344 S347 L352 D353 K356
Annotation score	1

Enzymatic activity

Enzyme Commision number

Gene Ontology

	Molecular Function
GO:0000149	SNARE binding
GO:0001540	amyloid-beta binding
GO:0004970	glutamate-gated receptor activity
GO:0004971	AMPA glutamate receptor activity
GO:0005230	extracellular ligand-gated monoatomic ion channel activity
GO:0005234	extracellularly glutamate-gated ion channel activity
GO:0005515	protein binding
GO:0008092	cytoskeletal protein binding
GO:0015276	ligand-gated monoatomic ion channel activity
GO:0015277	kainate selective glutamate receptor activity
GO:0019865	immunoglobulin binding
GO:0019901	protein kinase binding
GO:0022849	glutamate-gated calcium ion channel activity
GO:0030165	PDZ domain binding
GO:0035254	glutamate receptor binding
GO:0035255	ionotropic glutamate receptor binding
GO:0038023	signaling receptor activity
GO:0042802	identical protein binding
GO:0044877	protein-containing complex binding
GO:0097110	scaffold protein binding
GO:0099094	ligand-gated monoatomic cation channel activity
GO:0099507	ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential
GO:1904315	transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential

	Biological Process
GO:0001919	regulation of receptor recycling
GO:0006816	calcium ion transport
GO:0007268	chemical synaptic transmission
GO:0010226	response to lithium ion
GO:0019722	calcium-mediated signaling
GO:0021987	cerebral cortex development
GO:0031623	receptor internalization
GO:0034220	monoatomic ion transmembrane transport
GO:0035235	ionotropic glutamate receptor signaling pathway
GO:0035249	synaptic transmission, glutamatergic
GO:0045184	establishment of protein localization
GO:0050804	modulation of chemical synaptic transmission
GO:0050806	positive regulation of synaptic transmission
GO:0051262	protein tetramerization
GO:0051966	regulation of synaptic transmission, glutamatergic
GO:0060078	regulation of postsynaptic membrane potential
GO:0060079	excitatory postsynaptic potential
GO:0060992	response to fungicide
GO:0098655	monoatomic cation transmembrane transport
GO:0099505	regulation of presynaptic membrane potential
GO:1905430	cellular response to glycine
GO:1990416	cellular response to brain-derived neurotrophic factor stimulus

	Cellular Component
GO:0005783	endoplasmic reticulum
GO:0005886	plasma membrane
GO:0008021	synaptic vesicle
GO:0008328	ionotropic glutamate receptor complex
GO:0009986	cell surface
GO:0014069	postsynaptic density
GO:0016020	membrane
GO:0030424	axon
GO:0030425	dendrite
GO:0030426	growth cone
GO:0030672	synaptic vesicle membrane
GO:0032279	asymmetric synapse
GO:0032281	AMPA glutamate receptor complex
GO:0032590	dendrite membrane
GO:0032839	dendrite cytoplasm
GO:0032991	protein-containing complex
GO:0036477	somatodendritic compartment
GO:0042734	presynaptic membrane
GO:0043005	neuron projection
GO:0043025	neuronal cell body
GO:0043195	terminal bouton
GO:0043197	dendritic spine
GO:0043198	dendritic shaft
GO:0043204	perikaryon
GO:0044326	dendritic spine neck
GO:0044327	dendritic spine head
GO:0045202	synapse
GO:0045211	postsynaptic membrane
GO:0048787	presynaptic active zone membrane
GO:0097060	synaptic membrane
GO:0098685	Schaffer collateral - CA1 synapse
GO:0098793	presynapse
GO:0098839	postsynaptic density membrane
GO:0098978	glutamatergic synapse
GO:0099544	perisynaptic space
GO:0106033	spine synapse

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Molecular Function

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Cellular Component

External links

PDB	RCSB:7tno, PDBe:7tno, PDBj:7tno
PDBsum	7tno
PubMed	35444281
UniProt	P19491\|GRIA2_RAT Glutamate receptor 2 (Gene Name=Gria2); Q71RJ2

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