5AER
Neuronal calcium sensor-1 (NCS-1)from Rattus norvegicus complex with D2 dopamine receptor peptide from Homo sapiens
Replaces: 2YOUFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005245 | molecular_function | voltage-gated calcium channel activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005886 | cellular_component | plasma membrane |
A | 0008048 | molecular_function | calcium sensitive guanylate cyclase activator activity |
A | 0008427 | molecular_function | calcium-dependent protein kinase inhibitor activity |
A | 0010975 | biological_process | regulation of neuron projection development |
A | 0014069 | cellular_component | postsynaptic density |
A | 0019901 | molecular_function | protein kinase binding |
A | 0030424 | cellular_component | axon |
A | 0030425 | cellular_component | dendrite |
A | 0031045 | cellular_component | dense core granule |
A | 0044305 | cellular_component | calyx of Held |
A | 0045202 | cellular_component | synapse |
A | 0045921 | biological_process | positive regulation of exocytosis |
A | 0046872 | molecular_function | metal ion binding |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0050850 | biological_process | positive regulation of calcium-mediated signaling |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0098794 | cellular_component | postsynapse |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0099509 | biological_process | regulation of presynaptic cytosolic calcium ion concentration |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0099524 | cellular_component | postsynaptic cytosol |
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 200 |
Chain | Residue |
A | ASP73 |
A | ASN75 |
A | ASP77 |
A | ARG79 |
A | GLU81 |
A | GLU84 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 201 |
Chain | Residue |
A | TYR115 |
A | GLU120 |
A | ASP109 |
A | ASP111 |
A | ASP113 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 202 |
Chain | Residue |
A | ASP157 |
A | ASN159 |
A | ASP161 |
A | LYS163 |
A | GLU168 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE K A 203 |
Chain | Residue |
A | HOH2015 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DENKDGRIEfsEF |
Chain | Residue | Details |
A | ASP73-PHE85 | |
A | ASP109-MET121 | |
A | ASP157-PHE169 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
Chain | Residue | Details |
B | GLU432-SER443 | |
C | GLU432-SER443 | |
A | ASP77 | |
A | ARG79 | |
A | GLU84 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26535572 |
Chain | Residue | Details |
B | SER443 | |
C | SER443 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2, ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ |
Chain | Residue | Details |
A | ASP109 | |
A | ASP111 | |
A | ASP113 | |
A | TYR115 | |
A | GLU120 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2, ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ, ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP |
Chain | Residue | Details |
A | ASP157 | |
A | ASN159 | |
A | ASP161 | |
A | LYS163 | |
A | GLU168 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:10514519 |
Chain | Residue | Details |
A | GLY2 |