Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7X6I

Cryo-EM structure of the human TRPC5 ion channel in complex with G alpha i3 subunits, class1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0005262	molecular_function	calcium channel activity
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
A	0070588	biological_process	calcium ion transmembrane transport
B	0005216	molecular_function	monoatomic ion channel activity
B	0005262	molecular_function	calcium channel activity
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
B	0070588	biological_process	calcium ion transmembrane transport
C	0005216	molecular_function	monoatomic ion channel activity
C	0005262	molecular_function	calcium channel activity
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0055085	biological_process	transmembrane transport
C	0070588	biological_process	calcium ion transmembrane transport
D	0005216	molecular_function	monoatomic ion channel activity
D	0005262	molecular_function	calcium channel activity
D	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
D	0055085	biological_process	transmembrane transport
D	0070588	biological_process	calcium ion transmembrane transport
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0007165	biological_process	signal transduction
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
E	0019001	molecular_function	guanyl nucleotide binding
E	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
F	0003924	molecular_function	GTPase activity
F	0005525	molecular_function	GTP binding
F	0007165	biological_process	signal transduction
F	0007186	biological_process	G protein-coupled receptor signaling pathway
F	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
F	0019001	molecular_function	guanyl nucleotide binding
F	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
G	0003924	molecular_function	GTPase activity
G	0005525	molecular_function	GTP binding
G	0007165	biological_process	signal transduction
G	0007186	biological_process	G protein-coupled receptor signaling pathway
G	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
G	0019001	molecular_function	guanyl nucleotide binding
G	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
H	0003924	molecular_function	GTPase activity
H	0005525	molecular_function	GTP binding
H	0007165	biological_process	signal transduction
H	0007186	biological_process	G protein-coupled receptor signaling pathway
H	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
H	0019001	molecular_function	guanyl nucleotide binding
H	0031683	molecular_function	G-protein beta/gamma-subunit complex binding

Functional Information from PROSITE/UniProt

site_id	PS00962
Number of Residues	12
Details	RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. LiSLFTANSHLG

Chain	Residue	Details
A	LEU493-GLY504

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:2IHB, ECO:0007744\|PDB:2ODE, ECO:0007744\|PDB:2V4Z, ECO:0007744\|PDB:4G5O, ECO:0007744\|PDB:4G5R, ECO:0007744\|PDB:4G5S

Chain	Residue	Details
E	GLU43
H	GLU43
H	LEU175
H	ASN269
E	LEU175
E	ASN269
F	GLU43
F	LEU175
F	ASN269
G	GLU43
G	LEU175
G	ASN269

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:19478087, ECO:0007744\|PDB:2V4Z

Chain	Residue	Details
E	SER47
B	MET471-LEU491
B	MET513-ASN533
B	MET604-MET624
C	LEU331-SER351
C	PRO399-ILE419
C	MET438-VAL458
C	MET471-LEU491
C	MET513-ASN533
C	MET604-MET624
D	LEU331-SER351
E	THR181
D	PRO399-ILE419
D	MET438-VAL458
D	MET471-LEU491
D	MET513-ASN533
D	MET604-MET624
F	SER47
F	THR181
G	SER47
G	THR181
H	SER47
H	THR181
B	MET438-VAL458

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:2V4Z, ECO:0007744\|PDB:4G5O, ECO:0007744\|PDB:4G5R, ECO:0007744\|PDB:4G5S

Chain	Residue	Details
E	ASP150
D	PRO352-PRO398
D	LYS459-GLU470
D	GLY534-THR603
F	ASP150
G	ASP150
H	ASP150
B	LYS459-GLU470
B	GLY534-THR603
C	PRO352-PRO398
C	LYS459-GLU470
C	GLY534-THR603

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:19478087, ECO:0007744\|PDB:2V4Z

Chain	Residue	Details
E	ASP200
F	ASP200
G	ASP200
H	ASP200

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:2IHB, ECO:0007744\|PDB:2ODE, ECO:0007744\|PDB:2V4Z, ECO:0007744\|PDB:4G5O, ECO:0007744\|PDB:4G5R

Chain	Residue	Details
E	ALA326
F	ALA326
G	ALA326
H	ALA326

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
E	ARG178
F	ARG178
G	ARG178
H	ARG178

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
E	LEU204
F	LEU204
G	LEU204
H	LEU204

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
E	CYS351
F	CYS351
G	CYS351
H	CYS351

site_id	SWS_FT_FI9
Number of Residues	4
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:25255805

Chain	Residue	Details
E	GLY2
F	GLY2
G	GLY2
H	GLY2

site_id	SWS_FT_FI10
Number of Residues	4
Details	LIPID: S-palmitoyl cysteine => ECO:0000250

Chain	Residue	Details
E	CYS3
F	CYS3
G	CYS3
H	CYS3

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)