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

7BF2

Ca2+-Calmodulin in complex with human muscle form creatine kinase peptide in extended 1:2 binding mode

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000086biological_processG2/M transition of mitotic cell cycle
AAA0000922cellular_componentspindle pole
AAA0002027biological_processregulation of heart rate
AAA0005509molecular_functioncalcium ion binding
AAA0005513biological_processdetection of calcium ion
AAA0005515molecular_functionprotein binding
AAA0005576cellular_componentextracellular region
AAA0005634cellular_componentnucleus
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005813cellular_componentcentrosome
AAA0005819cellular_componentspindle
AAA0005829cellular_componentcytosol
AAA0005856cellular_componentcytoskeleton
AAA0005876cellular_componentspindle microtubule
AAA0005886cellular_componentplasma membrane
AAA0007186biological_processG protein-coupled receptor signaling pathway
AAA0008076cellular_componentvoltage-gated potassium channel complex
AAA0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
AAA0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
AAA0010856molecular_functionadenylate cyclase activator activity
AAA0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
AAA0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
AAA0016020cellular_componentmembrane
AAA0016240biological_processautophagosome membrane docking
AAA0019855molecular_functioncalcium channel inhibitor activity
AAA0019901molecular_functionprotein kinase binding
AAA0021762biological_processsubstantia nigra development
AAA0030017cellular_componentsarcomere
AAA0031432molecular_functiontitin binding
AAA0031514cellular_componentmotile cilium
AAA0031954biological_processpositive regulation of protein autophosphorylation
AAA0031982cellular_componentvesicle
AAA0032465biological_processregulation of cytokinesis
AAA0032516biological_processobsolete positive regulation of phosphoprotein phosphatase activity
AAA0032991cellular_componentprotein-containing complex
AAA0034704cellular_componentcalcium channel complex
AAA0035307biological_processobsolete positive regulation of protein dephosphorylation
AAA0035458biological_processcellular response to interferon-beta
AAA0043209cellular_componentmyelin sheath
AAA0043539molecular_functionprotein serine/threonine kinase activator activity
AAA0044305cellular_componentcalyx of Held
AAA0044325molecular_functiontransmembrane transporter binding
AAA0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
AAA0046872molecular_functionmetal ion binding
AAA0048306molecular_functioncalcium-dependent protein binding
AAA0050848biological_processregulation of calcium-mediated signaling
AAA0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
AAA0051592biological_processresponse to calcium ion
AAA0055117biological_processregulation of cardiac muscle contraction
AAA0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
AAA0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
AAA0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
AAA0071346biological_processcellular response to type II interferon
AAA0071902biological_processpositive regulation of protein serine/threonine kinase activity
AAA0072542molecular_functionprotein phosphatase activator activity
AAA0097225cellular_componentsperm midpiece
AAA0098901biological_processregulation of cardiac muscle cell action potential
AAA0099523cellular_componentpresynaptic cytosol
AAA0140056biological_processorganelle localization by membrane tethering
AAA0140238biological_processpresynaptic endocytosis
AAA1901020biological_processnegative regulation of calcium ion transmembrane transporter activity
AAA1901842biological_processnegative regulation of high voltage-gated calcium channel activity
AAA1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
AAA1902494cellular_componentcatalytic complex
AAA1905913biological_processnegative regulation of calcium ion export across plasma membrane
AAA1990456biological_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
AAAASP21-LEU33
AAAASP57-PHE69
AAAASP94-LEU106
AAAASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00564
ChainResidueDetails
CCCTHR313
AAAGLU68
DDDTHR313
AAAASP25
AAATHR27
AAAGLU32
AAAASP57
AAAASP59
AAAASN61
AAATHR63

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:29724949, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO
ChainResidueDetails
AAAASP94
AAAASP96
AAAASN98
AAATYR100
AAAGLU105

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
AAAASP130
AAAASP132
AAAASP134
AAAGLN136
AAAGLU141

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AAAALA2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
AAALYS22

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
AAATHR45

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AAASER82

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AAALYS95

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
AAATYR100

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AAASER102

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AAATHR111

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
AAALYS116

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AAATYR139

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
AAALYS22

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon