6AH4

Structure of human P2X3 receptor in complex with ATP and Ca2+ ion

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. GGvLGIkIgWvCDLDkawdqCiPkYsF

Chain	Residue	Details
A	GLY236-PHE262

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:27626375

Chain	Residue	Details
A	TRP21-PHE43
B	TRP21-PHE43
C	TRP21-PHE43

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site_id	SWS_FT_FI2
Number of Residues	834
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:27626375

Chain	Residue	Details
A	LEU44-ILE322
B	LEU44-ILE322
C	LEU44-ILE322

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site_id	SWS_FT_FI3
Number of Residues	54
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:27626375

Chain	Residue	Details
A	ILE323-ILE341
B	ILE323-ILE341
C	ILE323-ILE341

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site_id	SWS_FT_FI4
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269|PubMed:27626375, ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP

Chain	Residue	Details
A	LYS63
B	LYS299
C	LYS63
C	THR172
C	SER275
C	ASN279
C	LYS299
A	THR172
A	SER275
A	ASN279
A	LYS299
B	LYS63
B	THR172
B	SER275
B	ASN279

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0007744|PDB:5SVK

Chain	Residue	Details
A	ASN139
B	ASN139
C	ASN139

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site_id	SWS_FT_FI6
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ, ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS, ECO:0007744|PDB:5SVT

Chain	Residue	Details
A	ASN170
A	ASN290
B	ASN170
B	ASN290
C	ASN170
C	ASN290

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site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ, ECO:0007744|PDB:5SVS, ECO:0007744|PDB:5SVT

Chain	Residue	Details
A	ASN194
B	ASN194
C	ASN194

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