3IF7

Structure of Calmodulin complexed with its first endogenous inhibitor, sphingosylphosphorylcholine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000922	cellular_component	spindle pole
A	0002027	biological_process	regulation of heart rate
A	0005509	molecular_function	calcium ion binding
A	0005513	biological_process	detection of calcium ion
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005876	cellular_component	spindle microtubule
A	0008179	molecular_function	adenylate cyclase binding
A	0010856	molecular_function	adenylate cyclase activator activity
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0019901	molecular_function	protein kinase binding
A	0019904	molecular_function	protein domain specific binding
A	0030017	cellular_component	sarcomere
A	0031432	molecular_function	titin binding
A	0032465	biological_process	regulation of cytokinesis
A	0032991	cellular_component	protein-containing complex
A	0034704	cellular_component	calcium channel complex
A	0043209	cellular_component	myelin sheath
A	0043539	molecular_function	protein serine/threonine kinase activator activity
A	0044325	molecular_function	transmembrane transporter binding
A	0046872	molecular_function	metal ion binding
A	0051592	biological_process	response to calcium ion
A	0055117	biological_process	regulation of cardiac muscle contraction
A	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
A	0060316	biological_process	positive regulation of ryanodine-sensitive calcium-release channel activity
A	0072542	molecular_function	protein phosphatase activator activity
A	0097720	biological_process	calcineurin-mediated signaling
A	0098901	biological_process	regulation of cardiac muscle cell action potential
A	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 149

Chain	Residue
A	ASP20
A	ASP22
A	ASP24
A	THR26
A	GLU31
A	HOH160

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 150

Chain	Residue
A	THR62
A	GLU67
A	HOH157
A	ASP56
A	ASP58
A	ASN60

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 151

Chain	Residue
A	ASP93
A	ASP95
A	ASN97
A	TYR99
A	GLU104
A	HOH180

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 152

Chain	Residue
A	ASP129
A	ASP131
A	ASP133
A	GLN135
A	GLU140
A	HOH158

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SPU A 153

Chain	Residue
A	GLU11
A	MET76
A	ALA88
A	PHE92
A	GLU123
A	MET124
A	GLU127
A	PHE141
A	MET144
A	MET145
A	SPU154
A	SPU156

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SPU A 154

Chain	Residue
A	GLU11
A	LEU39
A	GLU87
A	MET124
A	SPU153
A	SPU155

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SPU A 155

Chain	Residue
A	PHE12
A	ALA15
A	LEU32
A	MET51
A	GLU54
A	VAL55
A	MET71
A	MET72
A	SPU154
A	SPU156

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SPU A 156

Chain	Residue
A	MET145
A	SPU153
A	SPU155

---

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
A	ASP20-LEU32
A	ASP56-PHE68
A	ASP93-LEU105
A	ASP129-PHE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
A	ASP20
A	GLU67
A	ASP93
A	ASP95
A	ASN97
A	TYR99
A	GLU104
A	ASP129
A	ASP131
A	ASP133
A	GLN135
A	ASP22
A	GLU140
A	ASP24
A	THR26
A	GLU31
A	ASP56
A	ASP58
A	ASN60
A	THR62

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:7356670

Chain	Residue	Details
A	ALA1

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS21

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29

Chain	Residue	Details
A	THR44

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	SER81
A	SER101

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS94

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	TYR99
A	TYR138

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	THR110

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS115

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384

Chain	Residue	Details
A	LYS21

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