7K4F

Cryo-EM structure of human TRPV6 in complex with (4- phenylcyclohexyl)piperazine inhibitor 31

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	0006816	biological_process	calcium ion transport
A	0016020	cellular_component	membrane
A	0055085	biological_process	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	0006816	biological_process	calcium ion transport
B	0016020	cellular_component	membrane
B	0055085	biological_process	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	0006816	biological_process	calcium ion transport
C	0016020	cellular_component	membrane
C	0055085	biological_process	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	0006816	biological_process	calcium 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	488
Details	TRANSMEM: Helical => ECO:0000305|PubMed:29258289

Chain	Residue	Details
A	TYR328-ILE348
B	GLU450-ALA469
B	LEU490-PHE512
B	ILE557-MET577
C	TYR328-ILE348
C	LEU386-PHE408
C	PRO424-ARG443
C	GLU450-ALA469
C	LEU490-PHE512
C	ILE557-MET577
D	TYR328-ILE348
A	LEU386-PHE408
D	LEU386-PHE408
D	PRO424-ARG443
D	GLU450-ALA469
D	LEU490-PHE512
D	ILE557-MET577
A	PRO424-ARG443
A	GLU450-ALA469
A	LEU490-PHE512
A	ILE557-MET577
B	TYR328-ILE348
B	LEU386-PHE408
B	PRO424-ARG443

---

site_id	SWS_FT_FI2
Number of Residues	252
Details	TOPO_DOM: Extracellular => ECO:0000305|PubMed:29258289

Chain	Residue	Details
A	TYR349-ARG385
C	LEU444-GLY449
C	GLN513-ASP525
C	ASN546-SER556
D	TYR349-ARG385
D	LEU444-GLY449
D	GLN513-ASP525
D	ASN546-SER556
A	LEU444-GLY449
A	GLN513-ASP525
A	ASN546-SER556
B	TYR349-ARG385
B	LEU444-GLY449
B	GLN513-ASP525
B	ASN546-SER556
C	TYR349-ARG385

---

site_id	SWS_FT_FI3
Number of Residues	132
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:29258289

Chain	Residue	Details
A	ARG409-GLY423
A	ARG470-ASP489
B	ARG409-GLY423
B	ARG470-ASP489
C	ARG409-GLY423
C	ARG470-ASP489
D	ARG409-GLY423
D	ARG470-ASP489

---

site_id	SWS_FT_FI4
Number of Residues	76
Details	INTRAMEM: Pore-forming => ECO:0000305|PubMed:29258289

Chain	Residue	Details
A	TYR526-ALA545
B	TYR526-ALA545
C	TYR526-ALA545
D	TYR526-ALA545

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:29258289

Chain	Residue	Details
A	ASP542
B	ASP542
C	ASP542
D	ASP542

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:Q9R186

Chain	Residue	Details
A	TYR161
B	TYR161
C	TYR161
D	TYR161

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN358
B	ASN358
C	ASN358
D	ASN358

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