5WC5

Structural insights into the potency of SK/IK channel positive modulators

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0005516	molecular_function	calmodulin binding
B	0006813	biological_process	potassium ion transport
B	0015269	molecular_function	calcium-activated potassium channel activity
B	0016020	cellular_component	membrane
B	0016286	molecular_function	small conductance calcium-activated potassium channel activity
R	0000086	biological_process	G2/M transition of mitotic cell cycle
R	0000922	cellular_component	spindle pole
R	0002027	biological_process	regulation of heart rate
R	0005246	molecular_function	calcium channel regulator activity
R	0005509	molecular_function	calcium ion binding
R	0005513	biological_process	detection of calcium ion
R	0005515	molecular_function	protein binding
R	0005576	cellular_component	extracellular region
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005737	cellular_component	cytoplasm
R	0005813	cellular_component	centrosome
R	0005819	cellular_component	spindle
R	0005829	cellular_component	cytosol
R	0005856	cellular_component	cytoskeleton
R	0005876	cellular_component	spindle microtubule
R	0005886	cellular_component	plasma membrane
R	0005929	cellular_component	cilium
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
R	0008076	cellular_component	voltage-gated potassium channel complex
R	0010856	molecular_function	adenylate cyclase activator activity
R	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
R	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
R	0016020	cellular_component	membrane
R	0016240	biological_process	autophagosome membrane docking
R	0019855	molecular_function	calcium channel inhibitor activity
R	0019901	molecular_function	protein kinase binding
R	0021762	biological_process	substantia nigra development
R	0030017	cellular_component	sarcomere
R	0030672	cellular_component	synaptic vesicle membrane
R	0031432	molecular_function	titin binding
R	0031514	cellular_component	motile cilium
R	0031982	cellular_component	vesicle
R	0032465	biological_process	regulation of cytokinesis
R	0032991	cellular_component	protein-containing complex
R	0034704	cellular_component	calcium channel complex
R	0035458	biological_process	cellular response to interferon-beta
R	0042995	cellular_component	cell projection
R	0043209	cellular_component	myelin sheath
R	0043539	molecular_function	protein serine/threonine kinase activator activity
R	0044305	cellular_component	calyx of Held
R	0044325	molecular_function	transmembrane transporter binding
R	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
R	0046872	molecular_function	metal ion binding
R	0048306	molecular_function	calcium-dependent protein binding
R	0050848	biological_process	regulation of calcium-mediated signaling
R	0051592	biological_process	response to calcium ion
R	0055117	biological_process	regulation of cardiac muscle contraction
R	0060291	biological_process	long-term synaptic potentiation
R	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
R	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
R	0071346	biological_process	cellular response to type II interferon
R	0072542	molecular_function	protein phosphatase activator activity
R	0097225	cellular_component	sperm midpiece
R	0097720	biological_process	calcineurin-mediated signaling
R	0098901	biological_process	regulation of cardiac muscle cell action potential
R	0099523	cellular_component	presynaptic cytosol
R	0140056	biological_process	organelle localization by membrane tethering
R	0140238	biological_process	presynaptic endocytosis
R	0141110	molecular_function	transporter inhibitor activity
R	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
R	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
R	1902494	cellular_component	catalytic complex
R	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
R	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue SO4 B 501

Chain	Residue
B	ALA447
B	ARG450
B	HOH609

---

site_id	AC2
Number of Residues	1
Details	binding site for residue SO4 B 502

Chain	Residue
B	HIS446

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 B 503

Chain	Residue
B	GOL505
B	ARG429
B	LYS451
B	HIS452
B	LYS455
B	SO4504

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 B 504

Chain	Residue
B	LYS451
B	ARG454
B	LYS455
B	SO4503

---

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL B 505

Chain	Residue
B	ASN437
B	LYS448
B	LYS451
B	HIS452
B	SO4503
B	HOH601

---

site_id	AC6
Number of Residues	6
Details	binding site for residue CA R 1001

Chain	Residue
R	ASP20
R	ASP22
R	ASP24
R	THR26
R	GLU31
R	HOH1168

---

site_id	AC7
Number of Residues	7
Details	binding site for residue CA R 1002

Chain	Residue
R	ASP56
R	ASP58
R	ASN60
R	THR62
R	GLU67
R	HOH1137
R	HOH1140

---

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 R 1003

Chain	Residue
B	LYS402
R	LYS77
R	THR79
R	HOH1105

---

site_id	AC9
Number of Residues	2
Details	binding site for residue SO4 R 1004

Chain	Residue
R	LYS30
R	ARG126

---

site_id	AD1
Number of Residues	7
Details	binding site for residue AJV R 1005

Chain	Residue
B	ALA477
B	LEU480
B	VAL481
R	MET51
R	VAL55
R	PHE68
R	MET71

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
R	ASP20-LEU32
R	ASP56-PHE68
R	ASP93-LEU105
R	ASP129-PHE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	35
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	35
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---