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5IRZ

Structure of TRPV1 determined in lipid nanodisc

Functional Information from GO Data
ChainGOidnamespacecontents
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
E0005216molecular_functionmonoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue 6O8 D 801
ChainResidue
DASN437
DVAL440
DPHE488
DARG491
DGLU513
DPHE516
DTYR554
DTYR555

site_idAC2
Number of Residues9
Detailsbinding site for residue 6ES D 802
ChainResidue
DSER510
DTYR511
DSER512
DTHR550
DARG557
DGLU570
DLEU699
DGLN700
DASP509

site_idAC3
Number of Residues3
Detailsbinding site for residue 6OE D 803
ChainResidue
B6OE803
DTYR631
EALA657

site_idAC4
Number of Residues1
Detailsbinding site for residue 6OE D 804
ChainResidue
DPHE655

site_idAC5
Number of Residues6
Detailsbinding site for residue 6OE D 805
ChainResidue
DTYR453
DTYR454
D6OE806
EPHE589
ESER629
E6OE806

site_idAC6
Number of Residues5
Detailsbinding site for residue 6OE D 806
ChainResidue
DTYR454
DGLY470
DPHE473
DARG474
D6OE805

site_idAC7
Number of Residues8
Detailsbinding site for residue 6O8 E 801
ChainResidue
EASN437
EVAL440
EPHE488
EARG491
EGLU513
EPHE516
ETYR554
ETYR555

site_idAC8
Number of Residues9
Detailsbinding site for residue 6ES E 802
ChainResidue
EASP509
ESER510
ETYR511
ESER512
ETHR550
EARG557
EGLU570
ELEU699
EGLN700

site_idAC9
Number of Residues1
Detailsbinding site for residue 6OE E 803
ChainResidue
EPHE655

site_idAD1
Number of Residues6
Detailsbinding site for residue 6OE E 804
ChainResidue
CPHE589
CSER629
C6OE805
ETYR453
ETYR454
E6OE805

site_idAD2
Number of Residues5
Detailsbinding site for residue 6OE E 805
ChainResidue
ETYR454
EGLY470
EPHE473
EARG474
E6OE804

site_idAD3
Number of Residues3
Detailsbinding site for residue 6OE E 806
ChainResidue
CALA657
D6OE805
ETYR631

site_idAD4
Number of Residues9
Detailsbinding site for residue 6ES B 802
ChainResidue
BASP509
BSER510
BTYR511
BSER512
BTHR550
BARG557
BGLU570
BLEU699
BGLN700

site_idAD5
Number of Residues6
Detailsbinding site for residue 6OE B 803
ChainResidue
BTYR453
BTYR454
B6OE804
DPHE589
DSER629
D6OE803

site_idAD6
Number of Residues5
Detailsbinding site for residue 6OE B 804
ChainResidue
BTYR454
BGLY470
BPHE473
BARG474
B6OE803

site_idAD7
Number of Residues3
Detailsbinding site for residue 6OE B 805
ChainResidue
BTYR631
C6OE803
DALA657

site_idAD8
Number of Residues1
Detailsbinding site for residue 6OE B 806
ChainResidue
BPHE655

site_idAD9
Number of Residues9
Detailsbinding site for residue 6ES C 802
ChainResidue
CASP509
CSER510
CTYR511
CSER512
CTHR550
CARG557
CGLU570
CLEU699
CGLN700

site_idAE1
Number of Residues6
Detailsbinding site for residue 6OE C 803
ChainResidue
B6OE805
CTYR453
CTYR454
C6OE804
BPHE589
BSER629

site_idAE2
Number of Residues5
Detailsbinding site for residue 6OE C 804
ChainResidue
CTYR454
CGLY470
CPHE473
CARG474
C6OE803

site_idAE3
Number of Residues3
Detailsbinding site for residue 6OE C 805
ChainResidue
BALA657
CTYR631
E6OE804

site_idAE4
Number of Residues1
Detailsbinding site for residue 6OE C 806
ChainResidue
CPHE655

site_idAE5
Number of Residues14
Detailsbinding site for Di-peptide 6O8 B 801 and ARG B 491
ChainResidue
BASN437
BVAL440
BTYR487
BPHE488
BPHE489
BPHE490
BGLY492
BILE493
BGLN494
BTYR495
BGLU513
BPHE516
BTYR554
BTYR555

site_idAE6
Number of Residues14
Detailsbinding site for Di-peptide 6O8 B 801 and PHE B 516
ChainResidue
BASN437
BVAL440
BPHE488
BARG491
BSER512
BGLU513
BILE514
BLEU515
BPHE517
BVAL518
BSER520
BASN551
BTYR554
BTYR555

site_idAE7
Number of Residues14
Detailsbinding site for Di-peptide 6O8 C 801 and PHE C 516
ChainResidue
CASN437
CVAL440
CPHE488
CARG491
CSER512
CGLU513
CILE514
CLEU515
CPHE517
CVAL518
CSER520
CASN551
CTYR554
CTYR555

site_idAE8
Number of Residues14
Detailsbinding site for Di-peptide 6O8 C 801 and ARG C 491
ChainResidue
CASN437
CVAL440
CTYR487
CPHE488
CPHE489
CPHE490
CGLY492
CILE493
CGLN494
CTYR495
CGLU513
CPHE516
CTYR554
CTYR555

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues560
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
DILE433-TYR453
EGLU536-THR556
EMET572-ILE599
EVAL658-VAL686
BILE433-TYR453
BTYR472-LEU497
BTYR511-PHE531
BGLU536-THR556
BMET572-ILE599
BVAL658-VAL686
CILE433-TYR453
DTYR472-LEU497
CTYR472-LEU497
CTYR511-PHE531
CGLU536-THR556
CMET572-ILE599
CVAL658-VAL686
DTYR511-PHE531
DGLU536-THR556
DMET572-ILE599
DVAL658-VAL686
EILE433-TYR453
ETYR472-LEU497
ETYR511-PHE531

site_idSWS_FT_FI2
Number of Residues184
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
DTYR454-ASP471
CTYR454-ASP471
CSER532-LYS535
CGLU600-PHE649
DSER532-LYS535
DGLU600-PHE649
ETYR454-ASP471
ESER532-LYS535
EGLU600-PHE649
BTYR454-ASP471
BSER532-LYS535
BGLU600-PHE649

site_idSWS_FT_FI3
Number of Residues104
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
ChainResidueDetails
DGLN498-SER510
DARG557-LYS571
EGLN498-SER510
EARG557-LYS571
BGLN498-SER510
BARG557-LYS571
CGLN498-SER510
CARG557-LYS571

site_idSWS_FT_FI4
Number of Residues88
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
ChainResidueDetails
DTYR627-PHE649
ETYR627-PHE649
BTYR627-PHE649
CTYR627-PHE649

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2PNN
ChainResidueDetails
DARG115
CARG115
CLYS155
CGLU210
DLYS155
DGLU210
EARG115
ELYS155
EGLU210
BARG115
BLYS155
BGLU210

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
ChainResidueDetails
DLYS160
CLYS160
CASN164
CTYR199
DASN164
DTYR199
ELYS160
EASN164
ETYR199
BLYS160
BASN164
BTYR199

site_idSWS_FT_FI7
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
ChainResidueDetails
DTYR511
CTYR511
CTHR550
CARG557
DTHR550
DARG557
ETYR511
ETHR550
EARG557
BTYR511
BTHR550
BARG557

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
DASP646
EASP646
BASP646
CASP646

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852
ChainResidueDetails
DSER116
ESER116
BSER116
CSER116

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
ChainResidueDetails
DTHR144
DTHR370
ETHR144
ETHR370
BTHR144
BTHR370
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
DSER502
ESER502
BSER502
CSER502

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912
ChainResidueDetails
DTHR704
ETHR704
BTHR704
CTHR704

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
ChainResidueDetails
DTYR627
ETYR627
BTYR627
CTYR627

225158

PDB entries from 2024-09-18

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