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3J5Q

Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008200molecular_functionion channel inhibitor activity
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005576cellular_componentextracellular region
C0008200molecular_functionion channel inhibitor activity
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
E0005216molecular_functionmonoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0055085biological_processtransmembrane transport
F0005576cellular_componentextracellular region
F0008200molecular_functionion channel inhibitor activity
G0005216molecular_functionmonoatomic ion channel activity
G0006811biological_processmonoatomic ion transport
G0016020cellular_componentmembrane
G0055085biological_processtransmembrane transport
H0005576cellular_componentextracellular region
H0008200molecular_functionion channel inhibitor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Involved in active face => ECO:0000250
ChainResidueDetails
DMET572-ILE599
BILE433-TYR453
CTRP30
FTRP30
HTRP30
DLEU681-GLU709
GLEU681-GLU709
ATRP30
BTYR472-LEU497
BTYR511-PHE531
BGLU536-THR556
BMET572-ILE599
BLEU681-GLU709
EILE433-TYR453
ETYR472-LEU497
ETYR511-PHE531
EGLU536-THR556
EMET572-ILE599
ELEU681-GLU709
GILE433-TYR453
GTYR472-LEU497
GTYR511-PHE531
GGLU536-THR556
GMET572-ILE599

site_idSWS_FT_FI2
Number of Residues184
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
DSER532-LYS535
DGLU600-PHE649
BTYR454-ASP471
DTYR454-ASP471
BSER532-LYS535
BGLU600-PHE649
ETYR454-ASP471
ESER532-LYS535
EGLU600-PHE649
GTYR454-ASP471
GSER532-LYS535
GGLU600-PHE649

site_idSWS_FT_FI3
Number of Residues104
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
DGLN498-SER510
DARG557-LYS571
BGLN498-SER510
BARG557-LYS571
EGLN498-SER510
EARG557-LYS571
GGLN498-SER510
GARG557-LYS571

site_idSWS_FT_FI4
Number of Residues88
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
ChainResidueDetails
DTHR650-ILE672
BTHR650-ILE672
ETHR650-ILE672
GTHR650-ILE672

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2PNN
ChainResidueDetails
BLYS155
BGLU210
EARG115
ELYS155
EGLU210
GARG115
GLYS155
GGLU210
DARG115
DLYS155
DGLU210
BARG115

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
ChainResidueDetails
BASN164
BTYR199
ELYS160
EASN164
ETYR199
GLYS160
GASN164
GTYR199
DLYS160
DASN164
DTYR199
BLYS160

site_idSWS_FT_FI7
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
ChainResidueDetails
BTHR550
BARG557
ETYR511
ETHR550
EARG557
GTYR511
GTHR550
GARG557
DTYR511
DTHR550
DARG557
BTYR511

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
DLEU669
BLEU669
ELEU669
GLEU669

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852
ChainResidueDetails
DSER116
BSER116
ESER116
GSER116

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
ChainResidueDetails
DTHR144
DTHR370
BTHR144
BTHR370
ETHR144
ETHR370
GTHR144
GTHR370

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
ChainResidueDetails
DSER502
BSER502
ESER502
GSER502

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912
ChainResidueDetails
DUNK728
BUNK728
EUNK728
GUNK728

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
ChainResidueDetails
DTYR627
BTYR627
ETYR627
GTYR627

218500

數據於2024-04-17公開中

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