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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7WZS

Crystal structure of Chromobacterium violaceum effector CopC in complex with host calmodulin and caspase-7

Functional Information from GO Data
ChainGOidnamespacecontents
A0005516molecular_functioncalmodulin binding
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0030430cellular_componenthost cell cytoplasm
A0052040biological_processsymbiont-mediated perturbation of host programmed cell death
A0090729molecular_functiontoxin activity
A0140740molecular_functionADP-riboxanase activity
B0001650cellular_componentfibrillar center
B0001778biological_processplasma membrane repair
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0007507biological_processheart development
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0009411biological_processresponse to UV
B0016485biological_processprotein processing
B0016787molecular_functionhydrolase activity
B0030163biological_processprotein catabolic process
B0042742biological_processdefense response to bacterium
B0043525biological_processpositive regulation of neuron apoptotic process
B0044346biological_processfibroblast apoptotic process
B0046513biological_processceramide biosynthetic process
B0051146biological_processstriated muscle cell differentiation
B0051402biological_processneuron apoptotic process
B0051604biological_processprotein maturation
B0070227biological_processlymphocyte apoptotic process
B0071222biological_processcellular response to lipopolysaccharide
B0071887biological_processleukocyte apoptotic process
B0072734biological_processcellular response to staurosporine
B0097194biological_processexecution phase of apoptosis
B1905686biological_processpositive regulation of plasma membrane repair
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
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005819cellular_componentspindle
C0005829cellular_componentcytosol
C0005876cellular_componentspindle microtubule
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008076cellular_componentvoltage-gated potassium channel complex
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
C0016240biological_processautophagosome membrane docking
C0019855molecular_functioncalcium channel inhibitor activity
C0019901molecular_functionprotein kinase binding
C0021762biological_processsubstantia nigra development
C0030017cellular_componentsarcomere
C0030672cellular_componentsynaptic vesicle membrane
C0031432molecular_functiontitin binding
C0031514cellular_componentmotile cilium
C0031982cellular_componentvesicle
C0032465biological_processregulation of cytokinesis
C0032991cellular_componentprotein-containing complex
C0034704cellular_componentcalcium channel complex
C0035458biological_processcellular response to interferon-beta
C0043209cellular_componentmyelin sheath
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0044305cellular_componentcalyx of Held
C0044325molecular_functiontransmembrane transporter binding
C0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
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
C0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
C0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
C0071346biological_processcellular response to type II interferon
C0072542molecular_functionprotein phosphatase activator activity
C0097225cellular_componentsperm midpiece
C0097720biological_processcalcineurin-mediated signaling
C0098901biological_processregulation of cardiac muscle cell action potential
C0099523cellular_componentpresynaptic cytosol
C0140056biological_processorganelle localization by membrane tethering
C0140238biological_processpresynaptic endocytosis
C0141110molecular_functiontransporter inhibitor activity
C1901842biological_processnegative regulation of high voltage-gated calcium channel 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
C1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
CASP21-LEU33
CASP57-PHE69
CASP94-LEU106
CASP130-PHE142
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HtnaaCfaCiLLSHG
ChainResidueDetails
BHIS131-GLY145
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsRepeat: {"description":"ANK 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues32
DetailsRepeat: {"description":"ANK 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00023","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XN4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues11
DetailsRegion: {"description":"Loop L1","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11701129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16916640","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Involved in allosteric regulation","evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581639","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues5
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_FI14
Number of Residues5
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_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
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_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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