2X0G
X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
B | 0000922 | cellular_component | spindle pole |
B | 0002027 | biological_process | regulation of heart rate |
B | 0005246 | molecular_function | calcium channel regulator activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005513 | biological_process | detection of calcium ion |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005813 | cellular_component | centrosome |
B | 0005819 | cellular_component | spindle |
B | 0005829 | cellular_component | cytosol |
B | 0005876 | cellular_component | spindle microtubule |
B | 0005886 | cellular_component | plasma membrane |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0008076 | cellular_component | voltage-gated potassium channel complex |
B | 0010856 | molecular_function | adenylate cyclase activator activity |
B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
B | 0016020 | cellular_component | membrane |
B | 0016240 | biological_process | autophagosome membrane docking |
B | 0019855 | molecular_function | calcium channel inhibitor activity |
B | 0019901 | molecular_function | protein kinase binding |
B | 0021762 | biological_process | substantia nigra development |
B | 0030017 | cellular_component | sarcomere |
B | 0030672 | cellular_component | synaptic vesicle membrane |
B | 0031432 | molecular_function | titin binding |
B | 0031514 | cellular_component | motile cilium |
B | 0031982 | cellular_component | vesicle |
B | 0032465 | biological_process | regulation of cytokinesis |
B | 0032991 | cellular_component | protein-containing complex |
B | 0034704 | cellular_component | calcium channel complex |
B | 0035458 | biological_process | cellular response to interferon-beta |
B | 0043209 | cellular_component | myelin sheath |
B | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
B | 0044305 | cellular_component | calyx of Held |
B | 0044325 | molecular_function | transmembrane transporter binding |
B | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
B | 0046872 | molecular_function | metal ion binding |
B | 0048306 | molecular_function | calcium-dependent protein binding |
B | 0050848 | biological_process | regulation of calcium-mediated signaling |
B | 0051592 | biological_process | response to calcium ion |
B | 0055117 | biological_process | regulation of cardiac muscle contraction |
B | 0060291 | biological_process | long-term synaptic potentiation |
B | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
B | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
B | 0071346 | biological_process | cellular response to type II interferon |
B | 0072542 | molecular_function | protein phosphatase activator activity |
B | 0097225 | cellular_component | sperm midpiece |
B | 0097720 | biological_process | calcineurin-mediated signaling |
B | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
B | 0099523 | cellular_component | presynaptic cytosol |
B | 0140056 | biological_process | organelle localization by membrane tethering |
B | 0140238 | biological_process | presynaptic endocytosis |
B | 0141110 | molecular_function | transporter inhibitor activity |
B | 1901842 | biological_process | negative regulation of high voltage-gated calcium channel activity |
B | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
B | 1902494 | cellular_component | catalytic complex |
B | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
B | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 1146 |
Chain | Residue |
B | ASP93 |
B | ASP95 |
B | ASN97 |
B | TYR99 |
B | GLU104 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1147 |
Chain | Residue |
B | GLU140 |
B | HOH2021 |
B | ASP129 |
B | ASP131 |
B | ASP133 |
B | GLN135 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1148 |
Chain | Residue |
B | ASP20 |
B | ASP22 |
B | ASP24 |
B | THR26 |
B | GLU31 |
B | HOH2003 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 1149 |
Chain | Residue |
B | ASP56 |
B | ASP58 |
B | ASN60 |
B | THR62 |
B | GLU67 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1321 |
Chain | Residue |
A | ARG47 |
A | LYS50 |
A | SER57 |
A | ARG58 |
A | HOH2150 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1322 |
Chain | Residue |
A | ARG63 |
A | HIS166 |
A | ASN172 |
A | HOH2151 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
Chain | Residue | Details |
B | ASP20-LEU32 | |
B | ASP56-PHE68 | |
B | ASP93-LEU105 | |
B | ASP129-PHE141 |
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......FIKK |
Chain | Residue | Details |
A | LEU19-LYS46 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML |
Chain | Residue | Details |
A | ILE135-LEU147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 262 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | Region: {"description":"Autoinhibitory domain","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 13 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by RPS6KA1 and RPS6KA3","evidences":[{"source":"PubMed","id":"16213824","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"11579085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15729359","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17056602","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 35 |
Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 10 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 5 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Modified 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |