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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IS0

Structure of TRPV1 in complex with capsazepine, determined in lipid nanodisc

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0005216	molecular_function	monoatomic ion channel activity
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
C	0005216	molecular_function	monoatomic ion channel activity
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0055085	biological_process	transmembrane transport
D	0005216	molecular_function	monoatomic ion channel activity
D	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
D	0055085	biological_process	transmembrane transport
E	0005216	molecular_function	monoatomic ion channel activity
E	0006811	biological_process	monoatomic ion transport
E	0016020	cellular_component	membrane
E	0055085	biological_process	transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue 6ET C 801

Chain	Residue
B	LEU669
C	TYR511
C	SER512
C	LEU515
C	PHE543
C	THR550
C	ASN551
C	LEU553
C	GLU570

site_id	AC2
Number of Residues	9
Details	binding site for residue 6ET B 801

Chain	Residue
B	TYR511
B	SER512
B	LEU515
B	PHE543
B	THR550
B	ASN551
B	LEU553
B	GLU570
E	LEU669

site_id	AC3
Number of Residues	9
Details	binding site for residue 6ET D 801

Chain	Residue
C	LEU669
D	TYR511
D	SER512
D	LEU515
D	PHE543
D	THR550
D	ASN551
D	LEU553
D	GLU570

site_id	AC4
Number of Residues	9
Details	binding site for residue 6ET E 801

Chain	Residue
D	LEU669
E	TYR511
E	SER512
E	LEU515
E	PHE543
E	THR550
E	ASN551
E	LEU553
E	GLU570

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	560
Details	TRANSMEM: Helical => ECO:0000269\|PubMed:24305160, ECO:0000269\|PubMed:27281200

Chain	Residue	Details
C	ILE433-TYR453
B	GLU536-THR556
B	MET572-ILE599
B	VAL658-VAL686
D	ILE433-TYR453
D	TYR472-LEU497
D	TYR511-PHE531
D	GLU536-THR556
D	MET572-ILE599
D	VAL658-VAL686
E	ILE433-TYR453
C	TYR472-LEU497
E	TYR472-LEU497
E	TYR511-PHE531
E	GLU536-THR556
E	MET572-ILE599
E	VAL658-VAL686
C	TYR511-PHE531
C	GLU536-THR556
C	MET572-ILE599
C	VAL658-VAL686
B	ILE433-TYR453
B	TYR472-LEU497
B	TYR511-PHE531

site_id	SWS_FT_FI2
Number of Residues	184
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:24305160, ECO:0000269\|PubMed:27281200

Chain	Residue	Details
C	TYR454-ASP471
E	TYR454-ASP471
E	SER532-LYS535
E	GLU600-PHE649
C	SER532-LYS535
C	GLU600-PHE649
B	TYR454-ASP471
B	SER532-LYS535
B	GLU600-PHE649
D	TYR454-ASP471
D	SER532-LYS535
D	GLU600-PHE649

site_id	SWS_FT_FI3
Number of Residues	104
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:24305160, ECO:0000269\|PubMed:27281200

Chain	Residue	Details
C	GLN498-SER510
C	ARG557-LYS571
B	GLN498-SER510
B	ARG557-LYS571
D	GLN498-SER510
D	ARG557-LYS571
E	GLN498-SER510
E	ARG557-LYS571

site_id	SWS_FT_FI4
Number of Residues	88
Details	INTRAMEM: Pore-forming => ECO:0000269\|PubMed:24305160, ECO:0000269\|PubMed:27281200, ECO:0000305\|PubMed:10931826

Chain	Residue	Details
C	TYR627-PHE649
B	TYR627-PHE649
D	TYR627-PHE649
E	TYR627-PHE649

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:2PNN

Chain	Residue	Details
C	ARG115
E	ARG115
E	LYS155
E	GLU210
C	LYS155
C	GLU210
B	ARG115
B	LYS155
B	GLU210
D	ARG115
D	LYS155
D	GLU210

site_id	SWS_FT_FI6
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:2NYJ, ECO:0007744\|PDB:2PNN

Chain	Residue	Details
C	LYS160
E	LYS160
E	ASN164
E	TYR199
C	ASN164
C	TYR199
B	LYS160
B	ASN164
B	TYR199
D	LYS160
D	ASN164
D	TYR199

site_id	SWS_FT_FI7
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:27281200, ECO:0007744\|PDB:5IRX

Chain	Residue	Details
C	TYR511
E	TYR511
E	THR550
E	ARG557
C	THR550
C	ARG557
B	TYR511
B	THR550
B	ARG557
D	TYR511
D	THR550
D	ARG557

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q9R186

Chain	Residue	Details
C	ASP646
B	ASP646
D	ASP646
E	ASP646

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269\|PubMed:12194871, ECO:0000269\|PubMed:15471852

Chain	Residue	Details
C	SER116
B	SER116
D	SER116
E	SER116

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269\|PubMed:12194871

Chain	Residue	Details
C	THR144
C	THR370
B	THR144
B	THR370
D	THR144
D	THR370
E	THR144
E	THR370

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000269\|PubMed:11884385, ECO:0000269\|PubMed:12194871, ECO:0000269\|PubMed:14630912

Chain	Residue	Details
C	SER502
B	SER502
D	SER502
E	SER502

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:14630912

Chain	Residue	Details
C	THR704
B	THR704
D	THR704
E	THR704

site_id	SWS_FT_FI13
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:11683872

Chain	Residue	Details
C	TYR627
B	TYR627
D	TYR627
E	TYR627

226707

PDB entries from 2024-10-30

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