Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CI1

The Structure of Full-Length Kv Beta 2.1 Determined by Cryogenic Electron Microscopy

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005249	molecular_function	voltage-gated potassium channel activity
A	0005737	cellular_component	cytoplasm
A	0006813	biological_process	potassium ion transport
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
B	0005249	molecular_function	voltage-gated potassium channel activity
B	0005737	cellular_component	cytoplasm
B	0006813	biological_process	potassium ion transport
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
C	0005249	molecular_function	voltage-gated potassium channel activity
C	0005737	cellular_component	cytoplasm
C	0006813	biological_process	potassium ion transport
C	0016020	cellular_component	membrane
C	0055085	biological_process	transmembrane transport
D	0005249	molecular_function	voltage-gated potassium channel activity
D	0005737	cellular_component	cytoplasm
D	0006813	biological_process	potassium ion transport
D	0016020	cellular_component	membrane
D	0055085	biological_process	transmembrane transport
E	0005249	molecular_function	voltage-gated potassium channel activity
E	0005737	cellular_component	cytoplasm
E	0006813	biological_process	potassium ion transport
E	0016020	cellular_component	membrane
E	0055085	biological_process	transmembrane transport
F	0005249	molecular_function	voltage-gated potassium channel activity
F	0005737	cellular_component	cytoplasm
F	0006813	biological_process	potassium ion transport
F	0016020	cellular_component	membrane
F	0055085	biological_process	transmembrane transport
G	0005249	molecular_function	voltage-gated potassium channel activity
G	0005737	cellular_component	cytoplasm
G	0006813	biological_process	potassium ion transport
G	0016020	cellular_component	membrane
G	0055085	biological_process	transmembrane transport
H	0005249	molecular_function	voltage-gated potassium channel activity
H	0005737	cellular_component	cytoplasm
H	0006813	biological_process	potassium ion transport
H	0016020	cellular_component	membrane
H	0055085	biological_process	transmembrane transport

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:18672894

Chain	Residue	Details
A	TYR90
B	TYR90
C	TYR90
D	TYR90
E	TYR90
F	TYR90
G	TYR90
H	TYR90

site_id	SWS_FT_FI2
Number of Residues	112
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:16002581, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:18806782, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:20534430, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2A79, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3EAU, ECO:0007744\|PDB:3EB3, ECO:0007744\|PDB:3EB4, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:3LUT, ECO:0007744\|PDB:4JTA, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	THR56
A	LYS254
H	TRP57
H	GLN63
H	ASP85
H	SER188
H	GLN214
H	TRP243
H	SER244
H	LEU246
H	LYS254
H	ARG264
A	ARG264
H	SER325
H	GLN329
H	ASN333
A	SER325
A	GLN329
A	ASN333
B	THR56
B	TRP57
B	GLN63
B	ASP85
B	SER188
A	TRP57
B	GLN214
B	TRP243
B	SER244
B	LEU246
B	LYS254
B	ARG264
B	SER325
B	GLN329
B	ASN333
C	THR56
A	GLN63
C	TRP57
C	GLN63
C	ASP85
C	SER188
C	GLN214
C	TRP243
C	SER244
C	LEU246
C	LYS254
C	ARG264
A	ASP85
C	SER325
C	GLN329
C	ASN333
D	THR56
D	TRP57
D	GLN63
D	ASP85
D	SER188
D	GLN214
D	TRP243
A	SER188
D	SER244
D	LEU246
D	LYS254
D	ARG264
D	SER325
D	GLN329
D	ASN333
E	THR56
E	TRP57
E	GLN63
A	GLN214
E	ASP85
E	SER188
E	GLN214
E	TRP243
E	SER244
E	LEU246
E	LYS254
E	ARG264
E	SER325
E	GLN329
A	TRP243
E	ASN333
F	THR56
F	TRP57
F	GLN63
F	ASP85
F	SER188
F	GLN214
F	TRP243
F	SER244
F	LEU246
A	SER244
F	LYS254
F	ARG264
F	SER325
F	GLN329
F	ASN333
G	THR56
G	TRP57
G	GLN63
G	ASP85
G	SER188
A	LEU246
G	GLN214
G	TRP243
G	SER244
G	LEU246
G	LYS254
G	ARG264
G	SER325
G	GLN329
G	ASN333
H	THR56

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:4JTA

Chain	Residue	Details
A	ASN158
B	ASN158
C	ASN158
D	ASN158
E	ASN158
F	ASN158
G	ASN158
H	ASN158

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:16002581, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:18806782, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:20534430, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2A79, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3EB3, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:3LUT, ECO:0007744\|PDB:4JTA, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	ARG189
B	ARG189
C	ARG189
D	ARG189
E	ARG189
F	ARG189
G	ARG189
H	ARG189

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:16002581, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:18806782, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:20534430, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3EAU, ECO:0007744\|PDB:3EB3, ECO:0007744\|PDB:3EB4, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:3LUT, ECO:0007744\|PDB:4JTA, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	PRO245
B	PRO245
C	PRO245
D	PRO245
E	PRO245
F	PRO245
G	PRO245
H	PRO245

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:18806782, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3EAU, ECO:0007744\|PDB:3EB3, ECO:0007744\|PDB:3EB4, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:4JTA

Chain	Residue	Details
A	ALA247
B	ALA247
C	ALA247
D	ALA247
E	ALA247
F	ALA247
G	ALA247
H	ALA247

site_id	SWS_FT_FI7
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:16002581, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:18806782, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:20534430, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2A79, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3EAU, ECO:0007744\|PDB:3EB3, ECO:0007744\|PDB:3EB4, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:3LUT, ECO:0007744\|PDB:4JTA, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	CYS248
B	CYS248
C	CYS248
D	CYS248
E	CYS248
F	CYS248
G	CYS248
H	CYS248

site_id	SWS_FT_FI8
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	TYR262
B	TYR262
C	TYR262
D	TYR262
E	TYR262
F	TYR262
G	TYR262
H	TYR262

site_id	SWS_FT_FI9
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	GLY323
B	GLY323
C	GLY323
D	GLY323
E	GLY323
F	GLY323
G	GLY323
H	GLY323

site_id	SWS_FT_FI10
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10399921, ECO:0000269\|PubMed:10884227, ECO:0000269\|PubMed:16002581, ECO:0000269\|PubMed:18004376, ECO:0000269\|PubMed:20360102, ECO:0000269\|PubMed:20534430, ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:1EXB, ECO:0007744\|PDB:1QRQ, ECO:0007744\|PDB:2A79, ECO:0007744\|PDB:2R9R, ECO:0007744\|PDB:3LNM, ECO:0007744\|PDB:3LUT, ECO:0007744\|PDB:4JTA, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	GLU332
B	GLU332
C	GLU332
D	GLU332
E	GLU332
F	GLU332
G	GLU332
H	GLU332

site_id	SWS_FT_FI11
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:21357749

Chain	Residue	Details
A	SER112
B	SER112
C	SER112
D	SER112
E	SER112
F	SER112
G	SER112
H	SER112

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q13303

Chain	Residue	Details
A	LYS124
B	LYS124
C	LYS124
D	LYS124
E	LYS124
F	LYS124
G	LYS124
H	LYS124

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