9Z32

The structure of short splice variant (Q9UBL9-2) of human P2X2 receptor channel in lipid nanodiscs with Mg-ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001614	molecular_function	purinergic nucleotide receptor activity
A	0004931	molecular_function	extracellularly ATP-gated monoatomic cation channel activity
A	0005216	molecular_function	monoatomic ion channel activity
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0033198	biological_process	response to ATP
A	0098655	biological_process	monoatomic cation transmembrane transport
B	0001614	molecular_function	purinergic nucleotide receptor activity
B	0004931	molecular_function	extracellularly ATP-gated monoatomic cation channel activity
B	0005216	molecular_function	monoatomic ion channel activity
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0033198	biological_process	response to ATP
B	0098655	biological_process	monoatomic cation transmembrane transport
C	0001614	molecular_function	purinergic nucleotide receptor activity
C	0004931	molecular_function	extracellularly ATP-gated monoatomic cation channel activity
C	0005216	molecular_function	monoatomic ion channel activity
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0033198	biological_process	response to ATP
C	0098655	biological_process	monoatomic cation transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS01212
Number of Residues	27
Details	P2X_RECEPTOR ATP P2X receptors signature. GGvIGViInWdCDLDlpaseCnPkYsF

Chain	Residue	Details
A	GLY259-PHE285

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	819
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P56373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P56373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	39
Details	Region: {"description":"Pore-forming motif","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P56373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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