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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8YCP

structure of human trpv1 in complex with BC5

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	84
Details	TRANSMEM: Helical; Name=S1 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	ILE434-TYR455
B	ILE434-TYR455
C	ILE434-TYR455
D	ILE434-TYR455

site_id	SWS_FT_FI2
Number of Residues	208
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	ARG456-TYR472
C	HIS533-LYS535
C	ILE599-SER630
C	ASN653-PHE656
D	ARG456-TYR472
D	HIS533-LYS535
D	ILE599-SER630
D	ASN653-PHE656
A	HIS533-LYS535
A	ILE599-SER630
A	ASN653-PHE656
B	ARG456-TYR472
B	HIS533-LYS535
B	ILE599-SER630
B	ASN653-PHE656
C	ARG456-TYR472

site_id	SWS_FT_FI3
Number of Residues	96
Details	TRANSMEM: Helical; Name=S2 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	PHE473-LEU497
B	PHE473-LEU497
C	PHE473-LEU497
D	PHE473-LEU497

site_id	SWS_FT_FI4
Number of Residues	56
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	GLN498-SER510
A	ARG557-PHE559
B	GLN498-SER510
B	ARG557-PHE559
C	GLN498-SER510
C	ARG557-PHE559
D	GLN498-SER510
D	ARG557-PHE559

site_id	SWS_FT_FI5
Number of Residues	84
Details	TRANSMEM: Helical; Name=S3 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	TYR511-SER532
B	TYR511-SER532
C	TYR511-SER532
D	TYR511-SER532

site_id	SWS_FT_FI6
Number of Residues	80
Details	TRANSMEM: Helical; Name=S4 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	GLU536-THR556
B	GLU536-THR556
C	GLU536-THR556
D	GLU536-THR556

site_id	SWS_FT_FI7
Number of Residues	152
Details	TRANSMEM: Helical; Name=S5 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	GLN560-LEU598
B	GLN560-LEU598
C	GLN560-LEU598
D	GLN560-LEU598

site_id	SWS_FT_FI8
Number of Residues	84
Details	INTRAMEM: Pore-forming => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	LEU631-GLU652
B	LEU631-GLU652
C	LEU631-GLU652
D	LEU631-GLU652

site_id	SWS_FT_FI9
Number of Residues	104
Details	TRANSMEM: Helical; Name=S6 => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	LYS657-MET683
B	LYS657-MET683
C	LYS657-MET683
D	LYS657-MET683

site_id	SWS_FT_FI10
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	ARG116
B	ARG116
B	LYS156
B	LYS161
B	ASN165
B	TYR200
B	GLU211
B	TYR511
B	THR550
B	ARG557
C	ARG116
A	LYS156
C	LYS156
C	LYS161
C	ASN165
C	TYR200
C	GLU211
C	TYR511
C	THR550
C	ARG557
D	ARG116
D	LYS156
A	LYS161
D	LYS161
D	ASN165
D	TYR200
D	GLU211
D	TYR511
D	THR550
D	ARG557
A	ASN165
A	TYR200
A	GLU211
A	TYR511
A	THR550
A	ARG557

site_id	SWS_FT_FI11
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:37117175, ECO:0007744\|PDB:8GF8, ECO:0007744\|PDB:8GF9, ECO:0007744\|PDB:8GFA

Chain	Residue	Details
A	GLY644
B	GLY644
C	GLY644
D	GLY644

site_id	SWS_FT_FI12
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q9R186

Chain	Residue	Details
A	ASP647
B	ASP647
C	ASP647
D	ASP647

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA and PKD => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	SER117
B	SER117
C	SER117
D	SER117

site_id	SWS_FT_FI14
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	THR145
A	THR371
B	THR145
B	THR371
C	THR145
C	THR371
D	THR145
D	THR371

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	SER502
B	SER502
C	SER502
D	SER502

site_id	SWS_FT_FI16
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	THR705
B	THR705
C	THR705
D	THR705

site_id	SWS_FT_FI17
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250\|UniProtKB:O35433

Chain	Residue	Details
A	ASN604
B	ASN604
C	ASN604
D	ASN604

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PDB entries from 2025-06-11

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