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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PLM

Legionella pneumophila SidJ/ Calmodulin 2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0000086biological_processG2/M transition of mitotic cell cycle
C0000922cellular_componentspindle pole
C0002027biological_processregulation of heart rate
C0005246molecular_functioncalcium channel regulator activity
C0005509molecular_functioncalcium ion binding
C0005513biological_processdetection of calcium ion
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005819cellular_componentspindle
C0005856cellular_componentcytoskeleton
C0005876cellular_componentspindle microtubule
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008076cellular_componentvoltage-gated potassium channel complex
C0008179molecular_functionadenylate cyclase binding
C0010856molecular_functionadenylate cyclase activator activity
C0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0016020cellular_componentmembrane
C0019855molecular_functioncalcium channel inhibitor activity
C0019901molecular_functionprotein kinase binding
C0021762biological_processsubstantia nigra development
C0030017cellular_componentsarcomere
C0030672cellular_componentsynaptic vesicle membrane
C0031432molecular_functiontitin binding
C0031982cellular_componentvesicle
C0032465biological_processregulation of cytokinesis
C0032991cellular_componentprotein-containing complex
C0034704cellular_componentcalcium channel complex
C0043209cellular_componentmyelin sheath
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0044305cellular_componentcalyx of Held
C0044325molecular_functiontransmembrane transporter binding
C0046872molecular_functionmetal ion binding
C0048306molecular_functioncalcium-dependent protein binding
C0050848biological_processregulation of calcium-mediated signaling
C0051592biological_processresponse to calcium ion
C0055117biological_processregulation of cardiac muscle contraction
C0060291biological_processlong-term synaptic potentiation
C0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
C0072542molecular_functionprotein phosphatase activator activity
C0097225cellular_componentsperm midpiece
C0097720biological_processcalcineurin-mediated signaling
C0099523cellular_componentpresynaptic cytosol
C0140238biological_processpresynaptic endocytosis
C0141110molecular_functiontransporter inhibitor activity
C1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
C1902494cellular_componentcatalytic complex
C1905913biological_processnegative regulation of calcium ion export across plasma membrane
D0000086biological_processG2/M transition of mitotic cell cycle
D0000922cellular_componentspindle pole
D0002027biological_processregulation of heart rate
D0005246molecular_functioncalcium channel regulator activity
D0005509molecular_functioncalcium ion binding
D0005513biological_processdetection of calcium ion
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005856cellular_componentcytoskeleton
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
D0008179molecular_functionadenylate cyclase binding
D0010856molecular_functionadenylate cyclase activator activity
D0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0016020cellular_componentmembrane
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0030672cellular_componentsynaptic vesicle membrane
D0031432molecular_functiontitin binding
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044305cellular_componentcalyx of Held
D0044325molecular_functiontransmembrane transporter binding
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0050848biological_processregulation of calcium-mediated signaling
D0051592biological_processresponse to calcium ion
D0055117biological_processregulation of cardiac muscle contraction
D0060291biological_processlong-term synaptic potentiation
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0097720biological_processcalcineurin-mediated signaling
D0099523cellular_componentpresynaptic cytosol
D0140238biological_processpresynaptic endocytosis
D0141110molecular_functiontransporter inhibitor activity
D1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
D1902494cellular_componentcatalytic complex
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CA A 1001
ChainResidue
AASP542
AASP545
APOP1003
site_idAC2
Number of Residues3
Detailsbinding site for residue CA A 1002
ChainResidue
AASN534
AASP542
APOP1003
site_idAC3
Number of Residues9
Detailsbinding site for residue POP A 1003
ChainResidue
AASN534
AARG536
AASP542
ACA1001
ACA1002
AHOH1157
AARG352
ALYS367
ALYS370
site_idAC4
Number of Residues11
Detailsbinding site for residue AMP A 1004
ChainResidue
AHIS492
AHIS494
AARG505
ATYR506
AGLN507
AVAL510
AGLN517
AGLN519
AGLY521
AASN733
AARG734
site_idAC5
Number of Residues3
Detailsbinding site for residue CA B 1001
ChainResidue
BASP542
BASP545
BPOP1003
site_idAC6
Number of Residues3
Detailsbinding site for residue CA B 1002
ChainResidue
BASN534
BASP542
BPOP1003
site_idAC7
Number of Residues8
Detailsbinding site for residue POP B 1003
ChainResidue
BARG352
BLYS367
BASN534
BARG536
BASP542
BCA1001
BCA1002
BHOH1108
site_idAC8
Number of Residues11
Detailsbinding site for residue AMP B 1004
ChainResidue
BHIS492
BARG505
BTYR506
BGLN507
BVAL510
BGLN517
BPHE518
BGLN519
BGLY521
BASN733
BARG734
site_idAC9
Number of Residues4
Detailsbinding site for residue CA C 201
ChainResidue
CASP20
CASP22
CASP24
CTHR26
site_idAD1
Number of Residues5
Detailsbinding site for residue CA D 201
ChainResidue
DASP20
DASP22
DASP24
DTHR26
DHOH306
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
CASP20-LEU32
CASP56-PHE68
CASP93-LEU105
CASP129-PHE141
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31123136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OQQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7093203","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP30","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified 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"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240291

PDB entries from 2025-08-13

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