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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1K93

Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008294molecular_functioncalcium- and calmodulin-responsive adenylate cyclase activity
B0005576cellular_componentextracellular region
B0008294molecular_functioncalcium- and calmodulin-responsive adenylate cyclase activity
C0005576cellular_componentextracellular region
C0008294molecular_functioncalcium- and calmodulin-responsive adenylate cyclase activity
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
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
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
D0016240biological_processautophagosome membrane docking
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0030672cellular_componentsynaptic vesicle membrane
D0031432molecular_functiontitin binding
D0031514cellular_componentmotile cilium
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0035458biological_processcellular response to interferon-beta
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044305cellular_componentcalyx of Held
D0044325molecular_functiontransmembrane transporter binding
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
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
D0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0071346biological_processcellular response to type II interferon
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0097720biological_processcalcineurin-mediated signaling
D0098901biological_processregulation of cardiac muscle cell action potential
D0099523cellular_componentpresynaptic cytosol
D0140056biological_processorganelle localization by membrane tethering
D0140238biological_processpresynaptic endocytosis
D0141110molecular_functiontransporter inhibitor activity
D1901842biological_processnegative regulation of high voltage-gated calcium channel 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
D1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
E0000086biological_processG2/M transition of mitotic cell cycle
E0000922cellular_componentspindle pole
E0002027biological_processregulation of heart rate
E0005246molecular_functioncalcium channel regulator activity
E0005509molecular_functioncalcium ion binding
E0005513biological_processdetection of calcium ion
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005813cellular_componentcentrosome
E0005819cellular_componentspindle
E0005829cellular_componentcytosol
E0005876cellular_componentspindle microtubule
E0005886cellular_componentplasma membrane
E0007186biological_processG protein-coupled receptor signaling pathway
E0008076cellular_componentvoltage-gated potassium channel complex
E0010856molecular_functionadenylate cyclase activator activity
E0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
E0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
E0016020cellular_componentmembrane
E0016240biological_processautophagosome membrane docking
E0019855molecular_functioncalcium channel inhibitor activity
E0019901molecular_functionprotein kinase binding
E0021762biological_processsubstantia nigra development
E0030017cellular_componentsarcomere
E0030672cellular_componentsynaptic vesicle membrane
E0031432molecular_functiontitin binding
E0031514cellular_componentmotile cilium
E0031982cellular_componentvesicle
E0032465biological_processregulation of cytokinesis
E0032991cellular_componentprotein-containing complex
E0034704cellular_componentcalcium channel complex
E0035458biological_processcellular response to interferon-beta
E0043209cellular_componentmyelin sheath
E0043539molecular_functionprotein serine/threonine kinase activator activity
E0044305cellular_componentcalyx of Held
E0044325molecular_functiontransmembrane transporter binding
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0046872molecular_functionmetal ion binding
E0048306molecular_functioncalcium-dependent protein binding
E0050848biological_processregulation of calcium-mediated signaling
E0051592biological_processresponse to calcium ion
E0055117biological_processregulation of cardiac muscle contraction
E0060291biological_processlong-term synaptic potentiation
E0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
E0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
E0071346biological_processcellular response to type II interferon
E0072542molecular_functionprotein phosphatase activator activity
E0097225cellular_componentsperm midpiece
E0097720biological_processcalcineurin-mediated signaling
E0098901biological_processregulation of cardiac muscle cell action potential
E0099523cellular_componentpresynaptic cytosol
E0140056biological_processorganelle localization by membrane tethering
E0140238biological_processpresynaptic endocytosis
E0141110molecular_functiontransporter inhibitor activity
E1901842biological_processnegative regulation of high voltage-gated calcium channel activity
E1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
E1902494cellular_componentcatalytic complex
E1905913biological_processnegative regulation of calcium ion export across plasma membrane
E1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
F0000086biological_processG2/M transition of mitotic cell cycle
F0000922cellular_componentspindle pole
F0002027biological_processregulation of heart rate
F0005246molecular_functioncalcium channel regulator activity
F0005509molecular_functioncalcium ion binding
F0005513biological_processdetection of calcium ion
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005813cellular_componentcentrosome
F0005819cellular_componentspindle
F0005829cellular_componentcytosol
F0005876cellular_componentspindle microtubule
F0005886cellular_componentplasma membrane
F0007186biological_processG protein-coupled receptor signaling pathway
F0008076cellular_componentvoltage-gated potassium channel complex
F0010856molecular_functionadenylate cyclase activator activity
F0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
F0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
F0016020cellular_componentmembrane
F0016240biological_processautophagosome membrane docking
F0019855molecular_functioncalcium channel inhibitor activity
F0019901molecular_functionprotein kinase binding
F0021762biological_processsubstantia nigra development
F0030017cellular_componentsarcomere
F0030672cellular_componentsynaptic vesicle membrane
F0031432molecular_functiontitin binding
F0031514cellular_componentmotile cilium
F0031982cellular_componentvesicle
F0032465biological_processregulation of cytokinesis
F0032991cellular_componentprotein-containing complex
F0034704cellular_componentcalcium channel complex
F0035458biological_processcellular response to interferon-beta
F0043209cellular_componentmyelin sheath
F0043539molecular_functionprotein serine/threonine kinase activator activity
F0044305cellular_componentcalyx of Held
F0044325molecular_functiontransmembrane transporter binding
F0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
F0046872molecular_functionmetal ion binding
F0048306molecular_functioncalcium-dependent protein binding
F0050848biological_processregulation of calcium-mediated signaling
F0051592biological_processresponse to calcium ion
F0055117biological_processregulation of cardiac muscle contraction
F0060291biological_processlong-term synaptic potentiation
F0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
F0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
F0071346biological_processcellular response to type II interferon
F0072542molecular_functionprotein phosphatase activator activity
F0097225cellular_componentsperm midpiece
F0097720biological_processcalcineurin-mediated signaling
F0098901biological_processregulation of cardiac muscle cell action potential
F0099523cellular_componentpresynaptic cytosol
F0140056biological_processorganelle localization by membrane tethering
F0140238biological_processpresynaptic endocytosis
F0141110molecular_functiontransporter inhibitor activity
F1901842biological_processnegative regulation of high voltage-gated calcium channel activity
F1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
F1902494cellular_componentcatalytic complex
F1905913biological_processnegative regulation of calcium ion export across plasma membrane
F1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ALYS346
ALYS353
ASER354
ALYS372
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1003
ChainResidue
CLYS346
CLYS353
CSER354
CLYS372
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 801
ChainResidue
DASP131
DASP133
DGLN135
DGLU140
DASP129
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 802
ChainResidue
DASP93
DASP95
DASN97
DTYR99
DGLU104
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 803
ChainResidue
EASP129
EASP131
EASP133
EGLN135
EVAL136
EGLU140
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 804
ChainResidue
EASP93
EASP95
EASN97
ETYR99
EGLU104
site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 805
ChainResidue
FASP129
FASP131
FASP133
FGLN135
FGLU140
site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 806
ChainResidue
FASP93
FASP95
FASN97
FTYR99
FGLU104
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
DASP20-LEU32
DASP56-PHE68
DASP93-LEU105
DASP129-PHE141
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues165
DetailsRegion: {"description":"Catalytic CA1","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues417
DetailsRegion: {"description":"Catalytic CB","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues396
DetailsRegion: {"description":"Catalytic CA2","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15719022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15719022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XFW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues105
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues105
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues105
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues3
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_FI19
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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