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1LIN

CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0002027biological_processregulation of heart rate
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0008179molecular_functionadenylate cyclase binding
A0010856molecular_functionadenylate cyclase activator activity
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0031432molecular_functiontitin binding
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044325molecular_functiontransmembrane transporter binding
A0046872molecular_functionmetal ion binding
A0051592biological_processresponse to calcium ion
A0055117biological_processregulation of cardiac muscle contraction
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
A0072542molecular_functionprotein phosphatase activator activity
A0097720biological_processcalcineurin-mediated signaling
A0098901biological_processregulation of cardiac muscle cell action potential
A1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 149
ChainResidue
AASP20
AASP22
AASP24
ATHR26
AGLU31
AHOH173

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 150
ChainResidue
ATHR62
AGLU67
AHOH181
AASP56
AASP58
AASN60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 151
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH205

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 152
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH166

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TFP A 153
ChainResidue
AMET124
AGLU127
AVAL136
AMET144
ATFP154
ATFP155

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TFP A 154
ChainResidue
AGLU11
AGLU14
ALEU18
AMET109
AGLU114
ALEU116
AGLU120
AMET124
ATFP153
ATFP155

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TFP A 155
ChainResidue
AGLN8
AGLU11
AMET72
APHE92
AMET144
AMET145
AALA147
ATFP153
ATFP154

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TFP A 156
ChainResidue
AMET51
AILE52
AGLU54
AVAL55
AILE63
APHE68
AMET71

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP20-LEU32
AASP56-PHE68
AASP93-LEU105
AASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
ALYS21
APHE68
ALYS94
AGLY96
AGLY98
AILE100
ALEU105
AILE130
AGLY132
AGLY134
AVAL136
AGLY23
APHE141
AGLY25
AILE27
ALEU32
AALA57
AGLY59
AGLY61
AILE63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7356670
ChainResidueDetails
AASP2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASP22

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
AGLU45

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AGLU82
AALA102

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASP95

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AILE100
AGLU139

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASN111

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALEU116

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384
ChainResidueDetails
AASP22

227933

PDB entries from 2024-11-27

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