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7L2R

Cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-open 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
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0008289molecular_functionlipid binding
E0035821biological_processmodulation of process of another organism
E0090729molecular_functiontoxin activity
E0099106molecular_functionion channel regulator activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0008289molecular_functionlipid binding
F0035821biological_processmodulation of process of another organism
F0090729molecular_functiontoxin activity
F0099106molecular_functionion channel regulator activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSITE: Interacts with TRPV1 (reaches into the void formed by S4, S6 and pore-helix) => ECO:0000269|PubMed:27281200
ChainResidueDetails
FTRP11
BGLU536-THR556
BMET572-ILE599
BLEU681-GLU709
CILE433-TYR453
CTYR472-LEU497
CTYR511-PHE531
CGLU536-THR556
CMET572-ILE599
CLEU681-GLU709
DILE433-TYR453
FPHE27
DTYR472-LEU497
DTYR511-PHE531
DGLU536-THR556
DMET572-ILE599
DLEU681-GLU709
FTRP53
FPHE67
ETRP11
EPHE27
ETRP53
EPHE67
BTYR511-PHE531

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important residue for activation of TRPV1 => ECO:0000305|PubMed:26880553
ChainResidueDetails
FMET25
DTYR454-ASP471
DSER532-LYS535
DGLU600-PHE649
EMET25
AGLU600-PHE649
BTYR454-ASP471
BSER532-LYS535
BGLU600-PHE649
CTYR454-ASP471
CSER532-LYS535
CGLU600-PHE649

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important residue for activation of TRPV1 => ECO:0000269|PubMed:26880553
ChainResidueDetails
FLEU65
ELEU65
BGLN498-SER510
BARG557-LYS571
CGLN498-SER510
CARG557-LYS571
DGLN498-SER510
DARG557-LYS571

site_idSWS_FT_FI4
Number of Residues88
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
ChainResidueDetails
ATHR650-ILE672
BTHR650-ILE672
CTHR650-ILE672
DTHR650-ILE672

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2PNN
ChainResidueDetails
AARG115
DARG115
DLYS155
DGLU210
ALYS155
AGLU210
BARG115
BLYS155
BGLU210
CARG115
CLYS155
CGLU210

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
ChainResidueDetails
ALYS160
DLYS160
DASN164
DTYR199
AASN164
ATYR199
BLYS160
BASN164
BTYR199
CLYS160
CASN164
CTYR199

site_idSWS_FT_FI7
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
ChainResidueDetails
ATYR511
DTYR511
DTHR550
DARG557
ATHR550
AARG557
BTYR511
BTHR550
BARG557
CTYR511
CTHR550
CARG557

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
ALEU669
BLEU669
CLEU669
DLEU669

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852
ChainResidueDetails
ASER116
BSER116
CSER116
DSER116

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
ChainResidueDetails
ATHR144
ATHR370
BTHR144
BTHR370
CTHR144
CTHR370
DTHR144
DTHR370

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
ASER502
BSER502
CSER502
DSER502

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912
ChainResidueDetails
AGLN727
BGLN727
CGLN727
DGLN727

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
ChainResidueDetails
ATYR627
BTYR627
CTYR627
DTYR627

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PDB entries from 2024-08-21

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