Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EXB

STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002244	biological_process	hematopoietic progenitor cell differentiation
A	0004033	molecular_function	aldo-keto reductase (NADPH) activity
A	0005249	molecular_function	voltage-gated potassium channel activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0006813	biological_process	potassium ion transport
A	0008076	cellular_component	voltage-gated potassium channel complex
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0014069	cellular_component	postsynaptic density
A	0015459	molecular_function	potassium channel regulator activity
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0030424	cellular_component	axon
A	0031234	cellular_component	extrinsic component of cytoplasmic side of plasma membrane
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034702	cellular_component	monoatomic ion channel complex
A	0034705	cellular_component	potassium channel complex
A	0042995	cellular_component	cell projection
A	0043005	cellular_component	neuron projection
A	0043194	cellular_component	axon initial segment
A	0043679	cellular_component	axon terminus
A	0044224	cellular_component	juxtaparanode region of axon
A	0044325	molecular_function	transmembrane transporter binding
A	0044877	molecular_function	protein-containing complex binding
A	0045202	cellular_component	synapse
A	0045445	biological_process	myoblast differentiation
A	0050905	biological_process	neuromuscular process
A	0055085	biological_process	transmembrane transport
A	0055114	biological_process	obsolete oxidation-reduction process
A	0070995	biological_process	NADPH oxidation
A	0071805	biological_process	potassium ion transmembrane transport
A	0098839	cellular_component	postsynaptic density membrane
A	0098900	biological_process	regulation of action potential
A	0098978	cellular_component	glutamatergic synapse
A	1901379	biological_process	regulation of potassium ion transmembrane transport
A	1990031	cellular_component	pinceau fiber
A	2000008	biological_process	regulation of protein localization to cell surface
E	0005249	molecular_function	voltage-gated potassium channel activity
E	0006813	biological_process	potassium ion transport
E	0008076	cellular_component	voltage-gated potassium channel complex
E	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NDP A 1000

Chain	Residue
A	GLY55
A	ARG189
A	GLN214
A	TRP243
A	SER244
A	PRO245
A	LEU246
A	ALA247
A	CYS248
A	GLY249
A	SER252
A	THR56
A	LYS254
A	SER263
A	ARG264
A	LEU321
A	GLY323
A	SER325
A	GLN329
A	GLU332
A	ASN333
A	HOH1029
A	TRP57
A	HOH1052
A	HOH1160
A	GLN63
A	ASP85
A	TYR90
A	LYS118
A	ASN158
A	SER188

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:18672894

Chain	Residue	Details
A	TYR90

site_id	SWS_FT_FI2
Number of Residues	14
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
A	ARG264
A	SER325
A	GLN329
A	ASN333
A	TRP57
A	GLN63
A	ASP85
A	SER188
A	GLN214
A	TRP243
A	SER244
A	LEU246

site_id	SWS_FT_FI3
Number of Residues	1
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

site_id	SWS_FT_FI4
Number of Residues	1
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

site_id	SWS_FT_FI5
Number of Residues	1
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

site_id	SWS_FT_FI6
Number of Residues	1
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

site_id	SWS_FT_FI7
Number of Residues	1
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

site_id	SWS_FT_FI8
Number of Residues	1
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

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:23705070, ECO:0007744\|PDB:4JTC, ECO:0007744\|PDB:4JTD

Chain	Residue	Details
A	GLY323

site_id	SWS_FT_FI10
Number of Residues	1
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

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:21357749

Chain	Residue	Details
A	SER112

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q13303

Chain	Residue	Details
A	LYS124

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)