Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4G28

Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and EBIO-1

Functional Information from GO Data
ChainGOidnamespacecontents
B0005516molecular_functioncalmodulin binding
B0006813biological_processpotassium ion transport
B0015269molecular_functioncalcium-activated potassium channel activity
B0016020cellular_componentmembrane
B0016286molecular_functionsmall conductance calcium-activated potassium channel activity
R0000086biological_processG2/M transition of mitotic cell cycle
R0000922cellular_componentspindle pole
R0001975biological_processresponse to amphetamine
R0002027biological_processregulation of heart rate
R0005246molecular_functioncalcium channel regulator activity
R0005509molecular_functioncalcium ion binding
R0005513biological_processdetection of calcium ion
R0005515molecular_functionprotein binding
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005739cellular_componentmitochondrion
R0005813cellular_componentcentrosome
R0005819cellular_componentspindle
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0005876cellular_componentspindle microtubule
R0005929cellular_componentcilium
R0008076cellular_componentvoltage-gated potassium channel complex
R0008179molecular_functionadenylate cyclase binding
R0010856molecular_functionadenylate cyclase activator activity
R0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
R0016240biological_processautophagosome membrane docking
R0019855molecular_functioncalcium channel inhibitor activity
R0019901molecular_functionprotein kinase binding
R0019904molecular_functionprotein domain specific binding
R0030017cellular_componentsarcomere
R0030234molecular_functionenzyme regulator activity
R0030235molecular_functionnitric-oxide synthase regulator activity
R0030426cellular_componentgrowth cone
R0030672cellular_componentsynaptic vesicle membrane
R0031432molecular_functiontitin binding
R0031514cellular_componentmotile cilium
R0031800molecular_functiontype 3 metabotropic glutamate receptor binding
R0031966cellular_componentmitochondrial membrane
R0032465biological_processregulation of cytokinesis
R0032991cellular_componentprotein-containing complex
R0034704cellular_componentcalcium channel complex
R0035307biological_processpositive regulation of protein dephosphorylation
R0035458biological_processcellular response to interferon-beta
R0042995cellular_componentcell projection
R0043209cellular_componentmyelin sheath
R0043539molecular_functionprotein serine/threonine kinase activator activity
R0043548molecular_functionphosphatidylinositol 3-kinase binding
R0044325molecular_functiontransmembrane transporter binding
R0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
R0046872molecular_functionmetal ion binding
R0048306molecular_functioncalcium-dependent protein binding
R0050998molecular_functionnitric-oxide synthase binding
R0051592biological_processresponse to calcium ion
R0055117biological_processregulation of cardiac muscle contraction
R0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
R0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
R0071346biological_processcellular response to type II interferon
R0072542molecular_functionprotein phosphatase activator activity
R0090150biological_processestablishment of protein localization to membrane
R0090151biological_processestablishment of protein localization to mitochondrial membrane
R0097225cellular_componentsperm midpiece
R0098901biological_processregulation of cardiac muscle cell action potential
R0140056biological_processorganelle localization by membrane tethering
R1900242biological_processregulation of synaptic vesicle endocytosis
R1902494cellular_componentcatalytic complex
R1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
R2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG429
BLYS451
BHIS452
BLYS455

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA R 1001
ChainResidue
RHOH1101
RASP20
RASP22
RASP24
RTHR26
RGLU31

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA R 1002
ChainResidue
RASP56
RASP58
RASN60
RTHR62
RGLU67
RHOH1102

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL R 1003
ChainResidue
RILE100
RSER101
RGLU104
RGLN135
RHOH1119
RHOH1121
RHOH1129
RHOH1151

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 R 1004
ChainResidue
BLYS402
RASP78
RTHR79
RHOH1243

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 R 1005
ChainResidue
RLYS30
RARG126
RHOH1131
RHOH1191

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0W8 R 1006
ChainResidue
BLEU480
BVAL481
RMET51
RVAL55
RILE63
RPHE68
RMET71
RMET72

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
RASP20-LEU32
RASP56-PHE68
RASP93-LEU105
RASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
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
RASP20
RASP22
RASP24
RTHR26
RGLU31

site_idSWS_FT_FI2
Number of Residues5
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
RASP56
RASP58
RASN60
RTHR62
RGLU67

site_idSWS_FT_FI3
Number of Residues5
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
RASP93
RASP95
RASN97
RTYR99
RGLU104

site_idSWS_FT_FI4
Number of Residues5
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
RASP129
RASP131
RASP133
RGLN135
RGLU140

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8
ChainResidueDetails
RALA1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RLYS21

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
RTHR44

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RSER81

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RLYS94

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RTYR99

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RSER101

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RTHR110

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RLYS115

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
RTYR138

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
RLYS21

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon