Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WEL

Crystal structure of SU6656-bound calcium/calmodulin-dependent protein kinase II delta in complex with calmodulin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
D	0000922	cellular_component	spindle pole
D	0002027	biological_process	regulation of heart rate
D	0005246	molecular_function	calcium channel regulator activity
D	0005509	molecular_function	calcium ion binding
D	0005513	biological_process	detection of calcium ion
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005813	cellular_component	centrosome
D	0005819	cellular_component	spindle
D	0005829	cellular_component	cytosol
D	0005876	cellular_component	spindle microtubule
D	0005886	cellular_component	plasma membrane
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0008076	cellular_component	voltage-gated potassium channel complex
D	0010856	molecular_function	adenylate cyclase activator activity
D	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D	0016020	cellular_component	membrane
D	0016240	biological_process	autophagosome membrane docking
D	0019855	molecular_function	calcium channel inhibitor activity
D	0019901	molecular_function	protein kinase binding
D	0021762	biological_process	substantia nigra development
D	0030017	cellular_component	sarcomere
D	0031432	molecular_function	titin binding
D	0031514	cellular_component	motile cilium
D	0031982	cellular_component	vesicle
D	0032465	biological_process	regulation of cytokinesis
D	0032991	cellular_component	protein-containing complex
D	0034704	cellular_component	calcium channel complex
D	0035458	biological_process	cellular response to interferon-beta
D	0043209	cellular_component	myelin sheath
D	0043539	molecular_function	protein serine/threonine kinase activator activity
D	0044305	cellular_component	calyx of Held
D	0044325	molecular_function	transmembrane transporter binding
D	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
D	0046872	molecular_function	metal ion binding
D	0048306	molecular_function	calcium-dependent protein binding
D	0051592	biological_process	response to calcium ion
D	0055117	biological_process	regulation of cardiac muscle contraction
D	0060291	biological_process	long-term synaptic potentiation
D	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
D	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
D	0071346	biological_process	cellular response to type II interferon
D	0072542	molecular_function	protein phosphatase activator activity
D	0097225	cellular_component	sperm midpiece
D	0097720	biological_process	calcineurin-mediated signaling
D	0098901	biological_process	regulation of cardiac muscle cell action potential
D	0099523	cellular_component	presynaptic cytosol
D	0140056	biological_process	organelle localization by membrane tethering
D	0140238	biological_process	presynaptic endocytosis
D	0141110	molecular_function	transporter inhibitor activity
D	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
D	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
D	1902494	cellular_component	catalytic complex
D	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
D	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE K88 A 600

Chain	Residue
A	LEU20
A	EDO700
A	EDO701
A	VAL28
A	ALA41
A	LYS43
A	PHE90
A	ASP91
A	LEU92
A	VAL93
A	ASP157

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 700

Chain	Residue
A	K88600
A	HOH2289
A	HOH2290

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 701

Chain	Residue
A	GLU61
A	VAL74
A	PHE90
A	ALA156
A	ASP157
A	PHE158
A	K88600

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 702

Chain	Residue
A	GLU140
A	TYR180
A	HIS283
A	GLN285
A	HOH2292

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 703

Chain	Residue
A	HIS55
A	SER81
A	LYS147
A	PO4706

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 704

Chain	Residue
A	TYR14
A	LYS33
A	HIS77
A	PO4707
A	HOH2089
A	HOH2293
D	HOH2092

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 705

Chain	Residue
A	TYR205
A	PRO213
A	TYR231
A	ASP232
A	HOH2294

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 706

Chain	Residue
A	THR47
A	HIS55
A	SER81
A	GLU82
A	PHE85
A	HIS86
A	SER148
A	LYS149
A	EDO703
A	HOH2295

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 707

Chain	Residue
A	LYS69
A	ARG75
A	HIS77
A	EDO704
A	HOH2089
A	HOH2297

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 600

Chain	Residue
D	ASP21
D	ASP23
D	ASP25
D	THR27
D	GLU32
D	HOH2019

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 601

Chain	Residue
D	ASP57
D	ASP59
D	ASN61
D	THR63
D	GLU68
D	HOH2053

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 602

Chain	Residue
D	ASP94
D	ASP96
D	ASN98
D	TYR100
D	GLU105
D	HOH2104

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 603

Chain	Residue
D	ASP130
D	ASP132
D	ASP134
D	GLN136
D	GLU141
D	HOH2102

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
D	ASP21-LEU33
D	ASP57-PHE69
D	ASP94-LEU106
D	ASP130-PHE142

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCmkiptgqe..........YAAK

Chain	Residue	Details
A	LEU20-LYS43

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL

Chain	Residue	Details
A	ILE132-LEU144

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	258
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Region: {"description":"Autoinhibitory domain","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Region: {"description":"Calmodulin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16690701","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
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_FI11
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_FI12
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_FI13
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_FI14
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_FI15
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_FI16
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_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
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_FI19
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_FI20
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_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
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_FI23
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP136
A	GLU140

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP136
A	LYS138

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP136
A	LYS138
A	THR177

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP136
A	LYS138
A	ASN141

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