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5IRX

Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc

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 PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 6O8 A 801
ChainResidue
AASN437
AVAL440
ATYR487
APHE488
AARG491
AGLU513
APHE516
ATYR554
ATYR555

site_idAC2
Number of Residues5
Detailsbinding site for residue 6OE A 802
ChainResidue
ASER629
ATYR631
CTYR453
FALA66
FPHE67

site_idAC3
Number of Residues3
Detailsbinding site for residue 6OE A 803
ChainResidue
ASER532
AARG534
F6O9102

site_idAC4
Number of Residues17
Detailsbinding site for residue 6EU A 804
ChainResidue
ATYR511
ASER512
AILE514
ALEU515
AALA546
AMET547
ATHR550
AASN551
ALEU553
ATYR554
AARG557
AALA566
AILE569
AILE573
BPHE591
BILE668
BLEU669

site_idAC5
Number of Residues9
Detailsbinding site for residue 6O8 B 801
ChainResidue
BASN437
BVAL440
BTYR487
BPHE488
BARG491
BGLU513
BPHE516
BTYR554
BTYR555

site_idAC6
Number of Residues3
Detailsbinding site for residue 6OE B 802
ChainResidue
BSER532
BARG534
F6O9101

site_idAC7
Number of Residues17
Detailsbinding site for residue 6EU B 803
ChainResidue
BTYR511
BSER512
BILE514
BLEU515
BALA546
BMET547
BTHR550
BASN551
BLEU553
BTYR554
BARG557
BALA566
BILE569
BILE573
DPHE591
DILE668
DLEU669

site_idAC8
Number of Residues9
Detailsbinding site for residue 6O8 C 801
ChainResidue
CASN437
CVAL440
CTYR487
CPHE488
CARG491
CGLU513
CPHE516
CTYR554
CTYR555

site_idAC9
Number of Residues2
Detailsbinding site for residue 6OE C 802
ChainResidue
CARG534
E6O9101

site_idAD1
Number of Residues17
Detailsbinding site for residue 6EU C 803
ChainResidue
APHE591
AILE668
ALEU669
CTYR511
CSER512
CILE514
CLEU515
CALA546
CMET547
CTHR550
CASN551
CLEU553
CTYR554
CARG557
CALA566
CILE569
CILE573

site_idAD2
Number of Residues9
Detailsbinding site for residue 6O8 D 801
ChainResidue
DTYR555
DASN437
DVAL440
DTYR487
DPHE488
DARG491
DGLU513
DPHE516
DTYR554

site_idAD3
Number of Residues4
Detailsbinding site for residue 6O9 D 802
ChainResidue
DARG534
D6OE804
EVAL50
ETRP53

site_idAD4
Number of Residues5
Detailsbinding site for residue 6OE D 803
ChainResidue
BTYR453
DSER629
DTYR631
EALA66
EPHE67

site_idAD5
Number of Residues3
Detailsbinding site for residue 6OE D 804
ChainResidue
DSER532
DARG534
D6O9802

site_idAD6
Number of Residues17
Detailsbinding site for residue 6EU D 805
ChainResidue
CPHE591
CILE668
CLEU669
DTYR511
DSER512
DILE514
DLEU515
DALA546
DMET547
DTHR550
DASN551
DLEU553
DTYR554
DARG557
DALA566
DILE569
DILE573

site_idAD7
Number of Residues5
Detailsbinding site for residue 6O9 E 101
ChainResidue
CARG534
C6OE802
EGLU7
EVAL8
ETRP11

site_idAD8
Number of Residues4
Detailsbinding site for residue 6OE E 102
ChainResidue
CSER629
CTYR631
DTYR453
EGLU26

site_idAD9
Number of Residues4
Detailsbinding site for residue 6O9 F 101
ChainResidue
BARG534
B6OE802
FGLU7
FVAL8

site_idAE1
Number of Residues4
Detailsbinding site for residue 6O9 F 102
ChainResidue
AARG534
A6OE803
FGLU49
FVAL50

site_idAE2
Number of Residues4
Detailsbinding site for residue 6OE F 103
ChainResidue
ATYR453
BSER629
BTYR631
FGLU26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues560
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
AILE433-TYR453
ATYR472-LEU497
ATYR511-PHE531
AGLU536-THR556
AMET572-ILE599
AVAL658-VAL686
BILE433-TYR453
BTYR472-LEU497
BTYR511-PHE531
BGLU536-THR556
BMET572-ILE599
BVAL658-VAL686
CILE433-TYR453
CTYR472-LEU497
CTYR511-PHE531
CGLU536-THR556
CMET572-ILE599
CVAL658-VAL686
DILE433-TYR453
DTYR472-LEU497
DTYR511-PHE531
DMET572-ILE599
DVAL658-VAL686
DGLU536-THR556

site_idSWS_FT_FI2
Number of Residues184
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
ATYR454-ASP471
ASER532-LYS535
AGLU600-PHE649
BTYR454-ASP471
BSER532-LYS535
BGLU600-PHE649
CTYR454-ASP471
CSER532-LYS535
CGLU600-PHE649
DTYR454-ASP471
DSER532-LYS535
DGLU600-PHE649

site_idSWS_FT_FI3
Number of Residues104
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
AGLN498-SER510
AARG557-LYS571
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
ATYR627-PHE649
BTYR627-PHE649
CTYR627-PHE649
DTYR627-PHE649

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

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

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

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
AASP646
BASP646
CASP646
DASP646

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
ATHR704
BTHR704
CTHR704
DTHR704

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 2024-04-17

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