4EHQ
Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+/Calmodulin Displays a Unique Binding Mode
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 | 0001975 | biological_process | response to amphetamine |
A | 0002027 | biological_process | regulation of heart rate |
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 | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
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 | 0008076 | cellular_component | voltage-gated potassium channel complex |
A | 0008179 | molecular_function | adenylate cyclase binding |
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 | 0016240 | biological_process | autophagosome membrane docking |
A | 0019855 | molecular_function | calcium channel inhibitor activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030017 | cellular_component | sarcomere |
A | 0030235 | molecular_function | nitric-oxide synthase regulator activity |
A | 0030426 | cellular_component | growth cone |
A | 0030672 | cellular_component | synaptic vesicle membrane |
A | 0031432 | molecular_function | titin binding |
A | 0031514 | cellular_component | motile cilium |
A | 0031800 | molecular_function | type 3 metabotropic glutamate receptor binding |
A | 0031966 | cellular_component | mitochondrial membrane |
A | 0032465 | biological_process | regulation of cytokinesis |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034704 | cellular_component | calcium channel complex |
A | 0035307 | biological_process | obsolete positive regulation of protein dephosphorylation |
A | 0035458 | biological_process | cellular response to interferon-beta |
A | 0043209 | cellular_component | myelin sheath |
A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
A | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
A | 0044305 | cellular_component | calyx of Held |
A | 0044325 | molecular_function | transmembrane transporter binding |
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 | 0050998 | molecular_function | nitric-oxide synthase binding |
A | 0051592 | biological_process | response to calcium ion |
A | 0051649 | biological_process | establishment of localization in cell |
A | 0055117 | biological_process | regulation of cardiac muscle contraction |
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 | 0090150 | biological_process | establishment of protein localization to membrane |
A | 0090151 | biological_process | establishment of protein localization to mitochondrial membrane |
A | 0097225 | cellular_component | sperm midpiece |
A | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0099524 | cellular_component | postsynaptic cytosol |
A | 0140056 | biological_process | organelle localization by membrane tethering |
A | 0140238 | biological_process | presynaptic endocytosis |
A | 0150034 | cellular_component | distal axon |
A | 1900242 | biological_process | regulation of synaptic vesicle endocytosis |
A | 1902494 | cellular_component | catalytic complex |
A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
A | 2000300 | biological_process | regulation of synaptic vesicle exocytosis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 201 |
Chain | Residue |
A | ASP20 |
A | ASP22 |
A | ASP24 |
A | THR26 |
A | GLU31 |
A | HOH306 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 202 |
Chain | Residue |
A | GLN135 |
A | GLU140 |
A | HOH304 |
A | ASP129 |
A | ASP131 |
A | ASP133 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 203 |
Chain | Residue |
A | ASP93 |
A | ASP95 |
A | ASN97 |
A | TYR99 |
A | GLU104 |
A | HOH316 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 204 |
Chain | Residue |
A | ASP56 |
A | ASP58 |
A | ASN60 |
A | THR62 |
A | GLU67 |
A | HOH356 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GBL A 205 |
Chain | Residue |
A | GLU45 |
A | ALA46 |
A | GLY98 |
A | TYR99 |
A | ASN137 |
A | HOH369 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GBL A 206 |
Chain | Residue |
A | GLU45 |
A | PHE89 |
A | TYR138 |
A | HOH327 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GBL A 207 |
Chain | Residue |
A | ALA57 |
A | PRO66 |
A | GLU67 |
A | THR70 |
G | LYS78 |
G | HOH206 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GBL G 101 |
Chain | Residue |
A | MET109 |
A | LEU112 |
A | GLU114 |
G | LEU74 |
G | LYS78 |
G | LEU79 |
G | SER82 |
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 | ASP20-LEU32 | |
A | ASP56-PHE68 | |
A | ASP93-LEU105 | |
A | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11323678, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH |
Chain | Residue | Details |
A | ASP20 | |
A | ASP22 | |
A | ASP24 | |
A | THR26 | |
A | GLU31 |
Chain | Residue | Details |
A | ASP56 | |
A | ASP58 | |
A | ASN60 | |
A | THR62 | |
A | GLU67 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
Chain | Residue | Details |
A | ASP93 | |
A | ASP95 | |
A | ASN97 | |
A | TYR99 | |
A | GLU104 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
Chain | Residue | Details |
A | ASP129 | |
A | ASP131 | |
A | ASP133 | |
A | GLN135 | |
A | GLU140 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ALA1 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS21 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717 |
Chain | Residue | Details |
A | THR44 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | SER81 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS94 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | TYR99 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER101 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | THR110 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS115 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | TYR138 |
site_id | SWS_FT_FI15 |
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 | LYS21 |