4BY5
Crystal structure of Drosophila Frq2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0007268 | biological_process | chemical synaptic transmission |
A | 0007269 | biological_process | neurotransmitter secretion |
A | 0007528 | biological_process | neuromuscular junction development |
A | 0008021 | cellular_component | synaptic vesicle |
A | 0008048 | molecular_function | calcium sensitive guanylate cyclase activator activity |
A | 0016192 | biological_process | vesicle-mediated transport |
A | 0046872 | molecular_function | metal ion binding |
A | 0046928 | biological_process | regulation of neurotransmitter secretion |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0007268 | biological_process | chemical synaptic transmission |
B | 0007269 | biological_process | neurotransmitter secretion |
B | 0007528 | biological_process | neuromuscular junction development |
B | 0008021 | cellular_component | synaptic vesicle |
B | 0008048 | molecular_function | calcium sensitive guanylate cyclase activator activity |
B | 0016192 | biological_process | vesicle-mediated transport |
B | 0046872 | molecular_function | metal ion binding |
B | 0046928 | biological_process | regulation of neurotransmitter secretion |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0007268 | biological_process | chemical synaptic transmission |
C | 0007269 | biological_process | neurotransmitter secretion |
C | 0007528 | biological_process | neuromuscular junction development |
C | 0008021 | cellular_component | synaptic vesicle |
C | 0008048 | molecular_function | calcium sensitive guanylate cyclase activator activity |
C | 0016192 | biological_process | vesicle-mediated transport |
C | 0046872 | molecular_function | metal ion binding |
C | 0046928 | biological_process | regulation of neurotransmitter secretion |
D | 0005509 | molecular_function | calcium ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0007268 | biological_process | chemical synaptic transmission |
D | 0007269 | biological_process | neurotransmitter secretion |
D | 0007528 | biological_process | neuromuscular junction development |
D | 0008021 | cellular_component | synaptic vesicle |
D | 0008048 | molecular_function | calcium sensitive guanylate cyclase activator activity |
D | 0016192 | biological_process | vesicle-mediated transport |
D | 0046872 | molecular_function | metal ion binding |
D | 0046928 | biological_process | regulation of neurotransmitter secretion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1183 |
Chain | Residue |
A | ASP73 |
A | ASN75 |
A | ASP77 |
A | ALA79 |
A | GLU84 |
A | HOH2069 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1184 |
Chain | Residue |
A | TYR115 |
A | GLU120 |
A | HOH2081 |
A | ASP109 |
A | ASP111 |
A | ASP113 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1185 |
Chain | Residue |
A | ASP156 |
A | ASN158 |
A | ASP160 |
A | ARG162 |
A | GLU167 |
A | HOH2093 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1185 |
Chain | Residue |
B | ASP73 |
B | ASN75 |
B | ASP77 |
B | ALA79 |
B | GLU84 |
B | HOH2029 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1186 |
Chain | Residue |
B | ASP156 |
B | ASN158 |
B | ASP160 |
B | ARG162 |
B | GLU167 |
B | HOH2055 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 1185 |
Chain | Residue |
C | ASP73 |
C | ASN75 |
C | ASP77 |
C | ALA79 |
C | GLU84 |
C | HOH2020 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 1186 |
Chain | Residue |
C | ASP109 |
C | ASP111 |
C | ASP113 |
C | TYR115 |
C | GLU120 |
C | HOH2033 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 1187 |
Chain | Residue |
C | ASP156 |
C | ASN158 |
C | ASP160 |
C | ARG162 |
C | GLU167 |
C | HOH2036 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 1183 |
Chain | Residue |
D | ASP73 |
D | ASN75 |
D | ASP77 |
D | ALA79 |
D | GLU84 |
D | HOH2005 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 1184 |
Chain | Residue |
D | ASP156 |
D | ASN158 |
D | ASP160 |
D | ARG162 |
D | GLU167 |
D | HOH2017 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 1185 |
Chain | Residue |
D | ASP109 |
D | ASP111 |
D | ASP113 |
D | TYR115 |
D | GLU120 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1187 |
Chain | Residue |
B | ASP109 |
B | ASP111 |
B | ASP113 |
B | TYR115 |
B | GLU120 |
B | HOH2043 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 1188 |
Chain | Residue |
B | ARG70 |
B | ASP73 |
B | ASN76 |
B | HOH2021 |
B | HOH2022 |
B | HOH2026 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DENNDGAIEfeEF |
Chain | Residue | Details |
A | ASP73-PHE85 | |
A | ASP109-MET121 | |
A | ASP156-PHE168 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25074811, ECO:0000269|PubMed:28119500, ECO:0000269|PubMed:29966094, ECO:0007744|PDB:4BY4, ECO:0007744|PDB:4BY5, ECO:0007744|PDB:5AAN, ECO:0007744|PDB:5FYX, ECO:0007744|PDB:5G08, ECO:0007744|PDB:6EPA |
Chain | Residue | Details |
A | ASP73 | |
A | GLU120 | |
A | ASP156 | |
A | ASN158 | |
A | ASP160 | |
A | ARG162 | |
A | GLU167 | |
B | ASP73 | |
B | ASN75 | |
B | ASP77 | |
B | ALA79 | |
A | ASN75 | |
B | GLU84 | |
B | ASP109 | |
B | ASP111 | |
B | ASP113 | |
B | TYR115 | |
B | GLU120 | |
B | ASP156 | |
B | ASN158 | |
B | ASP160 | |
B | ARG162 | |
A | ASP77 | |
B | GLU167 | |
C | ASP73 | |
C | ASN75 | |
C | ASP77 | |
C | ALA79 | |
C | GLU84 | |
C | ASP109 | |
C | ASP111 | |
C | ASP113 | |
C | TYR115 | |
A | ALA79 | |
C | GLU120 | |
C | ASP156 | |
C | ASN158 | |
C | ASP160 | |
C | ARG162 | |
C | GLU167 | |
D | ASP73 | |
D | ASN75 | |
D | ASP77 | |
D | ALA79 | |
A | GLU84 | |
D | GLU84 | |
D | ASP109 | |
D | ASP111 | |
D | ASP113 | |
D | TYR115 | |
D | GLU120 | |
D | ASP156 | |
D | ASN158 | |
D | ASP160 | |
D | ARG162 | |
A | ASP109 | |
D | GLU167 | |
A | ASP111 | |
A | ASP113 | |
A | TYR115 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | LIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P62168 |
Chain | Residue | Details |
A | GLY2 | |
B | GLY2 | |
C | GLY2 | |
D | GLY2 |