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3SJQ

Crystal structure of a small conductance potassium channel splice variant complexed with calcium-calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000086biological_processG2/M transition of mitotic cell cycle
A0000922cellular_componentspindle pole
A0001975biological_processresponse to amphetamine
A0002027biological_processregulation of heart rate
A0005246molecular_functioncalcium channel regulator activity
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0008076cellular_componentvoltage-gated potassium channel complex
A0008179molecular_functionadenylate cyclase binding
A0010856molecular_functionadenylate cyclase activator activity
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0016240biological_processautophagosome membrane docking
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030426cellular_componentgrowth cone
A0030672cellular_componentsynaptic vesicle membrane
A0031432molecular_functiontitin binding
A0031514cellular_componentmotile cilium
A0031800molecular_functiontype 3 metabotropic glutamate receptor binding
A0031966cellular_componentmitochondrial membrane
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0035307biological_processpositive regulation of protein dephosphorylation
A0035458biological_processcellular response to interferon-beta
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0043548molecular_functionphosphatidylinositol 3-kinase binding
A0044325molecular_functiontransmembrane transporter binding
A0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050998molecular_functionnitric-oxide synthase binding
A0051592biological_processresponse to calcium ion
A0055117biological_processregulation of cardiac muscle contraction
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0071346biological_processcellular response to type II interferon
A0072542molecular_functionprotein phosphatase activator activity
A0090150biological_processestablishment of protein localization to membrane
A0090151biological_processestablishment of protein localization to mitochondrial membrane
A0097225cellular_componentsperm midpiece
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098901biological_processregulation of cardiac muscle cell action potential
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A0140056biological_processorganelle localization by membrane tethering
A1900242biological_processregulation of synaptic vesicle endocytosis
A1902494cellular_componentcatalytic complex
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
A2000300biological_processregulation of synaptic vesicle exocytosis
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0001975biological_processresponse to amphetamine
B0002027biological_processregulation of heart rate
B0005246molecular_functioncalcium channel regulator activity
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0008076cellular_componentvoltage-gated potassium channel complex
B0008179molecular_functionadenylate cyclase binding
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030426cellular_componentgrowth cone
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031800molecular_functiontype 3 metabotropic glutamate receptor binding
B0031966cellular_componentmitochondrial membrane
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050998molecular_functionnitric-oxide synthase binding
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0090150biological_processestablishment of protein localization to membrane
B0090151biological_processestablishment of protein localization to mitochondrial membrane
B0097225cellular_componentsperm midpiece
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098901biological_processregulation of cardiac muscle cell action potential
B0099523cellular_componentpresynaptic cytosol
B0099524cellular_componentpostsynaptic cytosol
B0140056biological_processorganelle localization by membrane tethering
B1900242biological_processregulation of synaptic vesicle endocytosis
B1902494cellular_componentcatalytic complex
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
B2000300biological_processregulation of synaptic vesicle exocytosis
C0005516molecular_functioncalmodulin binding
C0006813biological_processpotassium ion transport
C0015269molecular_functioncalcium-activated potassium channel activity
C0016020cellular_componentmembrane
C0016286molecular_functionsmall conductance calcium-activated potassium channel activity
D0005516molecular_functioncalmodulin binding
D0006813biological_processpotassium ion transport
D0015269molecular_functioncalcium-activated potassium channel activity
D0016020cellular_componentmembrane
D0016286molecular_functionsmall conductance calcium-activated potassium channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP20
AASP22
AASP24
ATHR26
AGLU31
AHOH155

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
ATHR62
AGLU67
AHOH156
AASP56
AASP58
AASN60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH157

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH158

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PHU A 2001
ChainResidue
APHE19
ALEU32
AMET51
AGLU54
AVAL55
AILE63
APHE68
AMET71
CALA480
CLEU483
CVAL484

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 149
ChainResidue
AASN97
ATYR99
AHOH165
BLYS21
BHOH154
BHOH258

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 150
ChainResidue
ALEU18
ALYS21
ASER38

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 151
ChainResidue
ALYS21
AHOH163
AHOH170
AHOH255
BASN97
BTYR99
BHOH166

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 152
ChainResidue
AASP64
AHOH277
BTHR79
DASN481
DVAL484
DASP485
DLYS488

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 153
ChainResidue
ATHR34
AARG37
AHOH289

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 154
ChainResidue
AARG106
AHIS107
ATHR110
AHOH312
CHOH159
CARG450
CARG454

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1001
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BGLU31
BHOH153

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BASP56
BASP58
BASN60
BTHR62
BGLU67
BHOH157

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1003
ChainResidue
BASP93
BASP95
BASN97
BTYR99
BGLU104
BHOH159

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1004
ChainResidue
BASP129
BASP131
BASP133
BGLN135
BGLU140
BHOH160

site_idBC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PHU B 2001
ChainResidue
BMET71
DALA480
DLEU483
DVAL484
BPHE19
BLEU32
BMET51
BGLU54
BVAL55
BILE63
BPHE68

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 149
ChainResidue
BLEU18
BLYS21
BSER38
BLEU39
BHOH253

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 150
ChainResidue
BTHR34
BARG37

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 151
ChainResidue
BALA102
BARG106
BHOH195

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 152
ChainResidue
BGLU123
BARG126
CARG467

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 5
ChainResidue
CLYS436
CASN437
CLYS448
CHIS452

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PHU C 2
ChainResidue
BALA57
BGLU67
BTHR70
BHOH196
CLEU486

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 2
ChainResidue
DLYS436
DASN437
DLYS448
DHIS452

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 3
ChainResidue
BARG106
BHIS107
DHOH281
DHOH308
DARG450

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 8
ChainResidue
AARG126
DARG467
DLYS470
DARG474

site_idCC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PHU D 1
ChainResidue
AALA57
ATHR70
DTHR482

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 Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
AASP20
BGLU31
AASP22
AASP24
ATHR26
AGLU31
BASP20
BASP22
BASP24
BTHR26

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
AASP56
BGLU67
AASP58
AASN60
ATHR62
AGLU67
BASP56
BASP58
BASN60
BTHR62

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
AASP93
BGLU104
AASP95
AASN97
ATYR99
AGLU104
BASP93
BASP95
BASN97
BTYR99

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
AASP129
BGLU140
AASP131
AASP133
AGLN135
AGLU140
BASP129
BASP131
BASP133
BGLN135

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8
ChainResidueDetails
AALA1
BALA1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS21
BLYS21

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
ATHR44
BTHR44

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ASER81
BSER81

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS94
BLYS94

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ATYR99
BTYR99

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER101
BSER101

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATHR110
BTHR110

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS115
BLYS115

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATYR138
BTYR138

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS21
BLYS21

221716

PDB entries from 2024-06-26

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