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7L2S

cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DILE433-TYR453
AILE433-TYR453
BILE433-TYR453
CILE433-TYR453

site_idSWS_FT_FI2
Number of Residues212
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DTYR454-ASP471
BSER532-LYS535
BGLU600-PHE649
BLEU673-ALA680
CTYR454-ASP471
CSER532-LYS535
CGLU600-PHE649
CLEU673-ALA680
DSER532-LYS535
DGLU600-PHE649
DLEU673-ALA680
ATYR454-ASP471
ASER532-LYS535
AGLU600-PHE649
ALEU673-ALA680
BTYR454-ASP471

site_idSWS_FT_FI3
Number of Residues100
DetailsTRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DTYR472-LEU497
ATYR472-LEU497
BTYR472-LEU497
CTYR472-LEU497

site_idSWS_FT_FI4
Number of Residues104
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DGLN498-SER510
DARG557-LYS571
AGLN498-SER510
AARG557-LYS571
BGLN498-SER510
BARG557-LYS571
CGLN498-SER510
CARG557-LYS571

site_idSWS_FT_FI5
Number of Residues80
DetailsTRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DTYR511-PHE531
ATYR511-PHE531
BTYR511-PHE531
CTYR511-PHE531

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DGLU536-THR556
AGLU536-THR556
BGLU536-THR556
CGLU536-THR556

site_idSWS_FT_FI7
Number of Residues108
DetailsTRANSMEM: Helical; Name=S5 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DMET572-ILE599
AMET572-ILE599
BMET572-ILE599
CMET572-ILE599

site_idSWS_FT_FI8
Number of Residues88
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DTHR650-ILE672
ATHR650-ILE672
BTHR650-ILE672
CTHR650-ILE672

site_idSWS_FT_FI9
Number of Residues112
DetailsTRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
ChainResidueDetails
DLEU681-GLU709
ALEU681-GLU709
BLEU681-GLU709
CLEU681-GLU709

site_idSWS_FT_FI10
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2PNN
ChainResidueDetails
DARG115
CARG115
CLYS155
CGLU210
DLYS155
DGLU210
AARG115
ALYS155
AGLU210
BARG115
BLYS155
BGLU210

site_idSWS_FT_FI11
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
ChainResidueDetails
DLYS160
CLYS160
CASN164
CTYR199
DASN164
DTYR199
ALYS160
AASN164
ATYR199
BLYS160
BASN164
BTYR199

site_idSWS_FT_FI12
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
ChainResidueDetails
DTYR511
CTYR511
CTHR550
CARG557
DTHR550
DARG557
ATYR511
ATHR550
AARG557
BTYR511
BTHR550
BARG557

site_idSWS_FT_FI13
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8NER1
ChainResidueDetails
DTYR666
ATYR666
BTYR666
CTYR666

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
DLEU669
ALEU669
BLEU669
CLEU669

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852
ChainResidueDetails
DSER116
ASER116
BSER116
CSER116

site_idSWS_FT_FI16
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
ChainResidueDetails
DTHR144
DTHR370
ATHR144
ATHR370
BTHR144
BTHR370
CTHR144
CTHR370

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
ChainResidueDetails
DSER502
ASER502
BSER502
CSER502

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912
ChainResidueDetails
DGLN727
AGLN727
BGLN727
CGLN727

site_idSWS_FT_FI19
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
ChainResidueDetails
DTYR627
ATYR627
BTYR627
CTYR627

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PDB entries from 2025-06-18

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