6RV2

Crystal structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1) in a closed conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005252	molecular_function	open rectifier potassium channel activity
A	0005267	molecular_function	potassium channel activity
A	0016020	cellular_component	membrane
A	0071805	biological_process	potassium ion transmembrane transport
B	0005252	molecular_function	open rectifier potassium channel activity
B	0005267	molecular_function	potassium channel activity
B	0016020	cellular_component	membrane
B	0071805	biological_process	potassium ion transmembrane transport
C	0005252	molecular_function	open rectifier potassium channel activity
C	0005267	molecular_function	potassium channel activity
C	0016020	cellular_component	membrane
C	0071805	biological_process	potassium ion transmembrane transport
D	0005252	molecular_function	open rectifier potassium channel activity
D	0005267	molecular_function	potassium channel activity
D	0016020	cellular_component	membrane
D	0071805	biological_process	potassium ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue K A 302

Chain	Residue
A	ILE94
B	GLY201
A	GLY95
A	ILE200
A	GLY201
A	K303
A	K309
B	ILE94
B	GLY95
B	ILE200

---

site_id	AC2
Number of Residues	10
Details	binding site for residue K A 303

Chain	Residue
A	THR93
A	ILE94
A	THR199
A	ILE200
A	K302
A	K304
B	THR93
B	ILE94
B	THR199
B	ILE200

---

site_id	AC3
Number of Residues	5
Details	binding site for residue K A 304

Chain	Residue
A	THR93
A	THR199
A	K303
B	THR93
B	THR199

---

site_id	AC4
Number of Residues	5
Details	binding site for residue Y01 A 305

Chain	Residue
A	ARG3
A	PHE238
A	PHE246
B	LEU115
B	PRO119

---

site_id	AC5
Number of Residues	6
Details	binding site for residue Y01 A 306

Chain	Residue
A	ARG79
A	PHE80
A	ALA81
A	GLN215
A	PHE225
B	PHE16

---

site_id	AC6
Number of Residues	2
Details	binding site for residue DMU A 307

Chain	Residue
A	ARG131
A	ILE132

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PC1 A 308

Chain	Residue
A	GLY105
A	PHE112
A	ALA176
B	ALA28

---

site_id	AC8
Number of Residues	9
Details	binding site for residue K A 309

Chain	Residue
A	GLY95
A	TYR96
A	GLY201
A	PHE202
A	K302
B	GLY95
B	TYR96
B	GLY201
B	PHE202

---

site_id	AC9
Number of Residues	3
Details	binding site for residue Y01 A 301

Chain	Residue
B	ARG3
B	PHE238
B	PHE246

---

site_id	AD1
Number of Residues	6
Details	binding site for residue Y01 B 302

Chain	Residue
A	PHE16
B	ARG79
B	PHE80
B	ALA81
B	GLN215
B	PHE225

---

site_id	AD2
Number of Residues	2
Details	binding site for residue DMU B 303

Chain	Residue
A	LYS2
B	ARG131

---

site_id	AD3
Number of Residues	4
Details	binding site for residue PC1 B 304

Chain	Residue
B	GLY105
B	PHE112
B	SER169
B	HIS180

---

site_id	AD4
Number of Residues	9
Details	binding site for residue K C 301

Chain	Residue
C	GLY95
C	TYR96
C	GLY201
C	PHE202
C	K302
D	GLY95
D	TYR96
D	GLY201
D	PHE202

---

site_id	AD5
Number of Residues	10
Details	binding site for residue K C 302

Chain	Residue
C	ILE94
C	GLY95
C	ILE200
C	GLY201
C	K301
C	K303
D	ILE94
D	GLY95
D	ILE200
D	GLY201

---

site_id	AD6
Number of Residues	10
Details	binding site for residue K C 303

Chain	Residue
C	THR93
C	ILE94
C	THR199
C	ILE200
C	K302
C	K304
D	THR93
D	ILE94
D	THR199
D	ILE200

---

site_id	AD7
Number of Residues	5
Details	binding site for residue K C 304

Chain	Residue
D	THR199
C	THR93
C	THR199
C	K303
D	THR93

---

site_id	AD8
Number of Residues	3
Details	binding site for residue Y01 C 305

Chain	Residue
C	PHE246
D	LEU115
D	PRO119

---

site_id	AD9
Number of Residues	1
Details	binding site for residue DMU C 306

Chain	Residue
C	ARG131

---

site_id	AE1
Number of Residues	5
Details	binding site for residue PC1 D 601

Chain	Residue
C	GLY105
C	PHE112
C	SER169
D	ALA28
D	LEU29

---

site_id	AE2
Number of Residues	4
Details	binding site for residue Y01 D 602

Chain	Residue
C	LEU115
D	ARG3
D	PHE238
D	PHE246

---

site_id	AE3
Number of Residues	5
Details	binding site for residue Y01 D 603

Chain	Residue
C	PHE16
D	ARG79
D	PHE80
D	ALA81
D	GLN215

---

site_id	AE4
Number of Residues	4
Details	binding site for residue PC1 D 604

Chain	Residue
D	GLY105
D	PHE112
D	SER169
D	HIS180

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	144
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	MET1-THR8
A	GLY129-ASN158
B	MET1-THR8
B	GLY129-ASN158
C	MET1-THR8
C	GLY129-ASN158
D	MET1-THR8
D	GLY129-ASN158

---

site_id	SWS_FT_FI2
Number of Residues	320
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	LEU9-LEU29
C	VAL108-LEU128
C	MET159-SER179
C	PHE223-VAL243
D	LEU9-LEU29
D	VAL108-LEU128
D	MET159-SER179
D	PHE223-VAL243
A	VAL108-LEU128
A	MET159-SER179
A	PHE223-VAL243
B	LEU9-LEU29
B	VAL108-LEU128
B	MET159-SER179
B	PHE223-VAL243
C	LEU9-LEU29

---

site_id	SWS_FT_FI3
Number of Residues	92
Details	INTRAMEM: Pore-forming; Name=Pore-forming 1 => ECO:0000255

Chain	Residue	Details
A	TRP78-PRO101
B	TRP78-PRO101
C	TRP78-PRO101
D	TRP78-PRO101

---

site_id	SWS_FT_FI4
Number of Residues	92
Details	INTRAMEM: Pore-forming; Name=Pore-forming 2 => ECO:0000255

Chain	Residue	Details
A	TRP184-ALA207
B	TRP184-ALA207
C	TRP184-ALA207
D	TRP184-ALA207

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN53
B	ASN53
C	ASN53
D	ASN53

---