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5SVS

Anomalous Mn2+ signal reveals a divalent cation-binding site in the head domain of the ATP-gated human P2X3 ion channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0001614molecular_functionpurinergic nucleotide receptor activity
A0001666biological_processresponse to hypoxia
A0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
A0005216molecular_functionmonoatomic ion channel activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0007165biological_processsignal transduction
A0007268biological_processchemical synaptic transmission
A0007274biological_processneuromuscular synaptic transmission
A0009266biological_processresponse to temperature stimulus
A0009408biological_processresponse to heat
A0009409biological_processresponse to cold
A0009612biological_processresponse to mechanical stimulus
A0009743biological_processresponse to carbohydrate
A0010524biological_processpositive regulation of calcium ion transport into cytosol
A0014832biological_processurinary bladder smooth muscle contraction
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0030424cellular_componentaxon
A0030432biological_processperistalsis
A0033198biological_processresponse to ATP
A0034220biological_processmonoatomic ion transmembrane transport
A0035590biological_processpurinergic nucleotide receptor signaling pathway
A0043005cellular_componentneuron projection
A0043235cellular_componentreceptor complex
A0046872molecular_functionmetal ion binding
A0048167biological_processregulation of synaptic plasticity
A0048266biological_processbehavioral response to pain
A0050804biological_processmodulation of chemical synaptic transmission
A0050850biological_processpositive regulation of calcium-mediated signaling
A0050909biological_processsensory perception of taste
A0051649biological_processestablishment of localization in cell
A0060079biological_processexcitatory postsynaptic potential
A0070207biological_processprotein homotrimerization
A0070588biological_processcalcium ion transmembrane transport
A0071318biological_processcellular response to ATP
A0098655biological_processmonoatomic cation transmembrane transport
A0098662biological_processinorganic cation transmembrane transport
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098686cellular_componenthippocampal mossy fiber to CA3 synapse
A0098794cellular_componentpostsynapse
Functional Information from PROSITE/UniProt
site_idPS01212
Number of Residues27
DetailsP2X_RECEPTOR ATP P2X receptors signature. GGvLGIkIgWvCDLDkawdqCiPkYsF
ChainResidueDetails
AGLY236-PHE262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:27626375
ChainResidueDetails
ATRP21-PHE43

site_idSWS_FT_FI2
Number of Residues278
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:27626375
ChainResidueDetails
ALEU44-ILE322

site_idSWS_FT_FI3
Number of Residues18
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:27626375
ChainResidueDetails
AILE323-ILE341

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:6AH5
ChainResidueDetails
ALYS63

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:6AH4, ECO:0007744|PDB:6AH5
ChainResidueDetails
ALYS65
ATHR172

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29674445, ECO:0007744|PDB:5YVE
ChainResidueDetails
AGLU111

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29674445, ECO:0000269|PubMed:31232692, ECO:0007744|PDB:5SVS, ECO:0007744|PDB:5YVE, ECO:0007744|PDB:6AH5
ChainResidueDetails
AASP158

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP, ECO:0007744|PDB:6AH4, ECO:0007744|PDB:6AH5
ChainResidueDetails
ASER275
AASN279
ALYS299

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP, ECO:0007744|PDB:6AH4, ECO:0007744|PDB:6AH5
ChainResidueDetails
AARG281

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0007744|PDB:5SVK
ChainResidueDetails
AASN139

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0000269|PubMed:29674445, ECO:0000269|PubMed:31232692, 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, ECO:0007744|PDB:5YVE, ECO:0007744|PDB:6AH4, ECO:0007744|PDB:6AH5
ChainResidueDetails
AASN170
AASN290

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27626375, ECO:0000269|PubMed:31232692, 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, ECO:0007744|PDB:6AH4, ECO:0007744|PDB:6AH5
ChainResidueDetails
AASN194

229183

PDB entries from 2024-12-18

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