2AL4

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH quisqualate and CX614.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2al4a_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d2al4b_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d2al4c_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d2al4d_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d2al4e_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d2al4f_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Glutamate receptor ligand binding core	Norway rat (Rattus norvegicus ) [TaxId: 10116 ], Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Lig_chan_3	e2al4A2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
A	SBP_bac_3_1st	e2al4A1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)
B	Lig_chan_3	e2al4B1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
B	SBP_bac_3_1st	e2al4B2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)
C	Lig_chan_3	e2al4C2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
C	SBP_bac_3_1st	e2al4C1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)
D	Lig_chan_3	e2al4D2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
D	SBP_bac_3_1st	e2al4D1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)
E	Lig_chan_3	e2al4E2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
E	SBP_bac_3_1st	e2al4E1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)
F	Lig_chan_3	e2al4F2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: Lig_chan_3	ECOD (1.6)
F	SBP_bac_3_1st	e2al4F1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_3_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
E	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
F	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00060	Ligand-gated ion channel (Lig_chan)	Ligand-gated ion channel	-	Family
A, B, C, D, E A, B, C, D, E, F	PF10613	Ligated ion channel L-glutamate- and glycine-binding site (Lig_chan-Glu_bd)	Ligated ion channel L-glutamate- and glycine-binding site	This region, sometimes called the S1 domain, is the luminal domain just upstream of the first, M1, transmembrane region of transmembrane ion-channel proteins, and it binds L-glutamate and glycine [2]. It is found in association with Lig_chan, Pfam:PF ...	This region, sometimes called the S1 domain, is the luminal domain just upstream of the first, M1, transmembrane region of transmembrane ion-channel proteins, and it binds L-glutamate and glycine [2]. It is found in association with Lig_chan, Pfam:PF00060.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Glutamate receptor 2	transmitter-gated monoatomic ion channel activity molecular transducer activity monoatomic ion channel activity glutamate-gated receptor activity neurotransmitter receptor activity ligand-gated channel activity AMPA glutamate receptor activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity transmembrane signaling receptor activity transporter activity glutamate receptor activity gated channel activity transmitter-gated monoatomic ion channel activity molecular transducer activity monoatomic ion channel activity glutamate-gated receptor activity neurotransmitter receptor activity ligand-gated channel activity AMPA glutamate receptor activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity transmembrane signaling receptor activity transporter activity glutamate receptor activity gated channel activity signaling receptor activity carboxylic acid transmembrane transporter activity ligand-gated monoatomic ion channel activity extracellular ligand-gated monoatomic ion channel activity amino acid transmembrane transporter activity channel activity transmitter-gated channel activity monoatomic ion transmembrane transporter activity organic acid transmembrane transporter activity transmembrane transporter activity organic anion transmembrane transporter activity amide binding amyloid-beta binding binding peptide binding cytoskeletal protein binding protein binding excitatory extracellular ligand-gated monoatomic ion channel activity extracellularly glutamate-gated ion channel activity protein-containing complex binding immunoglobulin binding identical protein binding monoatomic cation transmembrane transporter activity monoatomic cation channel activity ligand-gated monoatomic cation channel activity PDZ domain binding protein domain specific binding signaling receptor binding glutamate receptor binding ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential scaffold protein binding ligand-gated calcium channel activity calcium channel activity glutamate-gated calcium ion channel activity calcium ion transmembrane transporter activity metal ion transmembrane transporter activity ionotropic glutamate receptor binding SNARE binding kinase binding enzyme binding protein kinase binding transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential postsynaptic neurotransmitter receptor activity neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential sodium channel activity kainate selective glutamate receptor activity potassium ion transmembrane transporter activity ligand-gated sodium channel activity sodium ion transmembrane transporter activity potassium channel activity	localization import into cell receptor internalization transport cellular process receptor-mediated endocytosis endocytosis establishment of localization vesicle-mediated transport cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization localization import into cell receptor internalization transport cellular process receptor-mediated endocytosis endocytosis establishment of localization vesicle-mediated transport cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein tetramerization protein-containing complex assembly cellular component organization or biogenesis cellular response to endogenous stimulus cellular response to growth factor stimulus response to stimulus response to endogenous stimulus cellular response to nerve growth factor stimulus cellular response to brain-derived neurotrophic factor stimulus response to nerve growth factor response to growth factor trans-synaptic signaling regulation of biological process regulation of signaling regulation of cellular process modulation of chemical synaptic transmission signaling biological regulation cell-cell signaling chemical synaptic transmission cell communication synaptic signaling regulation of trans-synaptic signaling anterograde trans-synaptic signaling regulation of cell communication response to lithium ion response to metal ion response to chemical developmental process multicellular organismal process head development forebrain development animal organ development brain development nervous system development pallium development cerebral cortex development multicellular organism development central nervous system development anatomical structure development telencephalon development system development regulation of receptor recycling regulation of macromolecule metabolic process receptor recycling receptor metabolic process metabolic process macromolecule metabolic process regulation of metabolic process positive regulation of cell communication positive regulation of biological process positive regulation of synaptic transmission positive regulation of cellular process positive regulation of signaling protein localization establishment of protein localization cellular localization cellular macromolecule localization macromolecule localization response to antibiotic response to fungicide response to toxic substance cellular response to acid chemical cellular response to stimulus cellular response to nitrogen compound cellular response to amino acid stimulus response to glycine response to organonitrogen compound response to oxygen-containing compound response to nitrogen compound response to amino acid cellular response to glycine cellular response to oxygen-containing compound response to acid chemical cellular response to chemical stimulus cellular response to organonitrogen compound ligand-gated ion channel signaling pathway cell surface receptor signaling pathway ionotropic glutamate receptor signaling pathway glutamate receptor signaling pathway signal transduction synaptic transmission, glutamatergic regulation of synaptic transmission, glutamatergic	postsynaptic specialization membrane postsynaptic specialization synapse membrane plasma membrane cellular anatomical entity postsynaptic density membrane synaptic membrane cell periphery postsynaptic density postsynapse neuron to neuron synapse organelle cell junction postsynaptic specialization membrane postsynaptic specialization synapse membrane plasma membrane cellular anatomical entity postsynaptic density membrane synaptic membrane cell periphery postsynaptic density postsynapse neuron to neuron synapse organelle cell junction postsynaptic membrane asymmetric synapse plasma membrane region somatodendritic compartment cell body perikaryon neuronal cell body protein-containing complex plasma membrane protein complex membrane protein complex transporter complex receptor complex AMPA glutamate receptor complex ionotropic glutamate receptor complex neurotransmitter receptor complex transmembrane transporter complex plasma membrane signaling receptor complex monoatomic ion channel complex presynapse presynaptic membrane cell projection dendrite dendritic tree neuron projection plasma membrane bounded cell projection glutamatergic synapse extracellular region perisynaptic space spine synapse dendritic shaft neuron spine dendritic spine membrane-bounded organelle intracellular anatomical structure intracellular vesicle transport vesicle membrane endomembrane system intracellular organelle bounding membrane of organelle cytoplasmic vesicle vesicle membrane synaptic vesicle synaptic vesicle membrane vesicle transport vesicle exocytic vesicle membrane intracellular membrane-bounded organelle cytoplasmic vesicle membrane secretory vesicle cytoplasm organelle membrane exocytic vesicle axon dendritic spine neck axon terminus distal axon terminal bouton neuron projection terminus cell surface dendritic spine head growth cone site of polarized growth neuron projection cytoplasm cytoplasmic region plasma membrane bounded cell projection cytoplasm dendrite cytoplasm presynaptic active zone membrane presynaptic active zone cell leading edge leading edge membrane neuron projection membrane dendrite membrane cell projection membrane Schaffer collateral - CA1 synapse endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF	Domain
A, B, C, D, E A, B, C, D, E, F	IPR028082	Periplasmic binding protein-like I	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR001508	Ionotropic glutamate receptor, metazoa	Family
A, B, C, D, E A, B, C, D, E, F	IPR001828	Receptor, ligand binding region	Domain
A, B, C, D, E A, B, C, D, E, F	IPR001320	Ionotropic glutamate receptor, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR019594	Ionotropic glutamate receptor, L-glutamate and glycine-binding domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR015683	Ionotropic glutamate receptor	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.