9B36

Open state of kainate receptor GluK2 in complex with agonist glutamate and positive allosteric modulator BPAM344 bound to two concanavalin A dimers. Composite map.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0006811	biological_process	monoatomic ion transport
A	0015276	molecular_function	ligand-gated monoatomic ion channel activity
A	0016020	cellular_component	membrane
A	0038023	molecular_function	signaling receptor activity
B	0005216	molecular_function	monoatomic ion channel activity
B	0006811	biological_process	monoatomic ion transport
B	0015276	molecular_function	ligand-gated monoatomic ion channel activity
B	0016020	cellular_component	membrane
B	0038023	molecular_function	signaling receptor activity
C	0005216	molecular_function	monoatomic ion channel activity
C	0006811	biological_process	monoatomic ion transport
C	0015276	molecular_function	ligand-gated monoatomic ion channel activity
C	0016020	cellular_component	membrane
C	0038023	molecular_function	signaling receptor activity
D	0005216	molecular_function	monoatomic ion channel activity
D	0006811	biological_process	monoatomic ion transport
D	0015276	molecular_function	ligand-gated monoatomic ion channel activity
D	0016020	cellular_component	membrane
D	0038023	molecular_function	signaling receptor activity
E	0005509	molecular_function	calcium ion binding
E	0005536	molecular_function	D-glucose binding
E	0005537	molecular_function	D-mannose binding
E	0030145	molecular_function	manganese ion binding
E	0030246	molecular_function	carbohydrate binding
E	0042311	biological_process	vasodilation
E	0046872	molecular_function	metal ion binding
E	0097746	biological_process	blood vessel diameter maintenance
F	0005509	molecular_function	calcium ion binding
F	0005536	molecular_function	D-glucose binding
F	0005537	molecular_function	D-mannose binding
F	0030145	molecular_function	manganese ion binding
F	0030246	molecular_function	carbohydrate binding
F	0042311	biological_process	vasodilation
F	0046872	molecular_function	metal ion binding
F	0097746	biological_process	blood vessel diameter maintenance
G	0005509	molecular_function	calcium ion binding
G	0005536	molecular_function	D-glucose binding
G	0005537	molecular_function	D-mannose binding
G	0030145	molecular_function	manganese ion binding
G	0030246	molecular_function	carbohydrate binding
G	0042311	biological_process	vasodilation
G	0046872	molecular_function	metal ion binding
G	0097746	biological_process	blood vessel diameter maintenance
H	0005509	molecular_function	calcium ion binding
H	0005536	molecular_function	D-glucose binding
H	0005537	molecular_function	D-mannose binding
H	0030145	molecular_function	manganese ion binding
H	0030246	molecular_function	carbohydrate binding
H	0042311	biological_process	vasodilation
H	0046872	molecular_function	metal ion binding
H	0097746	biological_process	blood vessel diameter maintenance

Functional Information from PROSITE/UniProt

site_id	PS00307
Number of Residues	7
Details	LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT

Chain	Residue	Details
E	VAL5-THR11

---

site_id	PS00308
Number of Residues	10
Details	LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS

Chain	Residue	Details
E	LEU85-SER94

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	220
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	636
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15721240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17115050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S7Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"UniProtKB","id":"Q13002","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21791290","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	16
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15677325","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15677325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27737777","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---