Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8T10

TRPV1 in nanodisc bound with two LPA molecules in opposite monomers

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2432
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
BMET1-ARG432
DGLN498-SER510
DARG557-LYS571
CMET1-ARG432
CGLN498-SER510
CARG557-LYS571
BGLN498-SER510
BARG557-LYS571
AMET1-ARG432
AGLN498-SER510
AARG557-LYS571
DMET1-ARG432

site_idSWS_FT_FI2
Number of Residues560
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
BILE433-TYR453
AGLU536-THR556
AMET572-ILE599
ALEU681-GLU709
DILE433-TYR453
DTYR472-LEU497
DTYR511-PHE531
DGLU536-THR556
DMET572-ILE599
DLEU681-GLU709
CILE433-TYR453
BTYR472-LEU497
CTYR472-LEU497
CTYR511-PHE531
CGLU536-THR556
CMET572-ILE599
CLEU681-GLU709
BTYR511-PHE531
BGLU536-THR556
BMET572-ILE599
BLEU681-GLU709
AILE433-TYR453
ATYR472-LEU497
ATYR511-PHE531

site_idSWS_FT_FI3
Number of Residues184
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
BTYR454-ASP471
CTYR454-ASP471
CSER532-LYS535
CGLU600-PHE649
BSER532-LYS535
BGLU600-PHE649
ATYR454-ASP471
ASER532-LYS535
AGLU600-PHE649
DTYR454-ASP471
DSER532-LYS535
DGLU600-PHE649

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

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

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

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

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

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

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

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
BSER502
ASER502
DSER502
CSER502

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

site_idSWS_FT_FI13
Number of Residues8
DetailsMOD_RES: Phosphoserine; by PKA; in vitro => ECO:0000269|PubMed:12194871
ChainResidueDetails
BARG797
AARG797
DARG797
CARG797

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC/PRKCE and PKC/PRKCZ => ECO:0000269|PubMed:11884385
ChainResidueDetails
BPRO823
APRO823
DPRO823
CPRO823

site_idSWS_FT_FI15
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
ChainResidueDetails
BTYR627
ATYR627
DTYR627
CTYR627

220760

PDB entries from 2024-06-05

PDB statisticsPDBj update infoContact PDBjnumon