6XYR
Structure of the T4Lnano fusion protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
A | 0000922 | cellular_component | spindle pole |
A | 0002027 | biological_process | regulation of heart rate |
A | 0003796 | molecular_function | lysozyme activity |
A | 0003824 | molecular_function | catalytic activity |
A | 0005246 | molecular_function | calcium channel regulator activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005513 | biological_process | detection of calcium ion |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005813 | cellular_component | centrosome |
A | 0005819 | cellular_component | spindle |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005876 | cellular_component | spindle microtubule |
A | 0005886 | cellular_component | plasma membrane |
A | 0005929 | cellular_component | cilium |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007259 | biological_process | cell surface receptor signaling pathway via JAK-STAT |
A | 0008076 | cellular_component | voltage-gated potassium channel complex |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0010856 | molecular_function | adenylate cyclase activator activity |
A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
A | 0016020 | cellular_component | membrane |
A | 0016240 | biological_process | autophagosome membrane docking |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0019855 | molecular_function | calcium channel inhibitor activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0021762 | biological_process | substantia nigra development |
A | 0030017 | cellular_component | sarcomere |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0030672 | cellular_component | synaptic vesicle membrane |
A | 0031432 | molecular_function | titin binding |
A | 0031514 | cellular_component | motile cilium |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0031982 | cellular_component | vesicle |
A | 0032465 | biological_process | regulation of cytokinesis |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034704 | cellular_component | calcium channel complex |
A | 0035458 | biological_process | cellular response to interferon-beta |
A | 0042742 | biological_process | defense response to bacterium |
A | 0042995 | cellular_component | cell projection |
A | 0043209 | cellular_component | myelin sheath |
A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
A | 0044305 | cellular_component | calyx of Held |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
A | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
A | 0046872 | molecular_function | metal ion binding |
A | 0048306 | molecular_function | calcium-dependent protein binding |
A | 0050848 | biological_process | regulation of calcium-mediated signaling |
A | 0051592 | biological_process | response to calcium ion |
A | 0055117 | biological_process | regulation of cardiac muscle contraction |
A | 0060291 | biological_process | long-term synaptic potentiation |
A | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
A | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
A | 0071346 | biological_process | cellular response to type II interferon |
A | 0072542 | molecular_function | protein phosphatase activator activity |
A | 0097225 | cellular_component | sperm midpiece |
A | 0097720 | biological_process | calcineurin-mediated signaling |
A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0140056 | biological_process | organelle localization by membrane tethering |
A | 0140238 | biological_process | presynaptic endocytosis |
A | 0141110 | molecular_function | transporter inhibitor activity |
A | 1901842 | biological_process | negative regulation of high voltage-gated calcium channel activity |
A | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
A | 1902494 | cellular_component | catalytic complex |
A | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 401 |
Chain | Residue |
A | ASP233 |
A | ASP235 |
A | ASP237 |
A | THR239 |
A | GLU244 |
A | HOH533 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 402 |
Chain | Residue |
A | THR275 |
A | GLU280 |
A | HOH537 |
A | ASP269 |
A | ASP271 |
A | ASN273 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 403 |
Chain | Residue |
A | ASP342 |
A | ASP344 |
A | ASP346 |
A | GLN348 |
A | GLU353 |
A | HOH559 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA A 404 |
Chain | Residue |
A | ASP306 |
A | ASP308 |
A | ASN310 |
A | TYR312 |
A | GLU317 |
A | HOH605 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA A 405 |
Chain | Residue |
A | PHE149 |
A | SER152 |
A | ASN167 |
A | HOH611 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 406 |
Chain | Residue |
A | TYR123 |
A | ALA128 |
A | HOH590 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL A 407 |
Chain | Residue |
A | GLY148 |
A | SER171 |
A | HOH504 |
A | HOH545 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue GOL A 408 |
Chain | Residue |
A | ASP45 |
A | GLU46 |
A | GOL410 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | THR177 |
A | PRO178 |
A | ASN179 |
A | ARG180 |
A | GOL410 |
A | HOH544 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 410 |
Chain | Residue |
A | ILE44 |
A | ASP45 |
A | ARG183 |
A | GOL408 |
A | GOL409 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue CL A 411 |
Chain | Residue |
A | ASP82 |
A | ASN90 |
A | ARG154 |
A | ARG160 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CL A 412 |
Chain | Residue |
A | ASP127 |
A | LYS159 |
A | ASN273 |
A | HOH630 |
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 |
A | ASP233-LEU245 | |
A | ASP269-PHE281 | |
A | ASP306-LEU318 | |
A | ASP342-PHE354 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU46 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP55 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU67 | |
A | PHE139 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER152 | |
A | ASN167 |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 |
Chain | Residue | Details |
A | ASP233 | |
A | GLU280 | |
A | ASP235 | |
A | ASP237 | |
A | THR239 | |
A | GLU244 | |
A | ASP269 | |
A | ASP271 | |
A | ASN273 | |
A | THR275 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ASP306 | |
A | ASP308 | |
A | ASN310 | |
A | TYR312 | |
A | GLU317 |
site_id | SWS_FT_FI7 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 |
Chain | Residue | Details |
A | ASP342 | |
A | ASP344 | |
A | ASP346 | |
A | GLN348 | |
A | GLU353 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_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 |
Chain | Residue | Details |
A | ALA214 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS234 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 |
Chain | Residue | Details |
A | THR257 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER294 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS307 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR312 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER314 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR323 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | LYS328 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR351 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 |
Chain | Residue | Details |
A | LYS234 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU46 | proton shuttle (general acid/base) |
A | ASP55 | covalent catalysis |