5ER4
Crystal Structure of Calcium-loaded S100B bound to SC0025
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0005509 | molecular_function | calcium ion binding |
| X | 0005515 | molecular_function | protein binding |
| X | 0005576 | cellular_component | extracellular region |
| X | 0005615 | cellular_component | extracellular space |
| X | 0005634 | cellular_component | nucleus |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0006417 | biological_process | regulation of translation |
| X | 0007155 | biological_process | cell adhesion |
| X | 0007409 | biological_process | axonogenesis |
| X | 0007611 | biological_process | learning or memory |
| X | 0008270 | molecular_function | zinc ion binding |
| X | 0008284 | biological_process | positive regulation of cell population proliferation |
| X | 0016310 | biological_process | phosphorylation |
| X | 0019210 | molecular_function | kinase inhibitor activity |
| X | 0042803 | molecular_function | protein homodimerization activity |
| X | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| X | 0044548 | molecular_function | S100 protein binding |
| X | 0045917 | biological_process | positive regulation of complement activation |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0048143 | biological_process | astrocyte activation |
| X | 0048156 | molecular_function | tau protein binding |
| X | 0048306 | molecular_function | calcium-dependent protein binding |
| X | 0050786 | molecular_function | RAGE receptor binding |
| X | 0071638 | biological_process | negative regulation of monocyte chemotactic protein-1 production |
| X | 0097490 | biological_process | sympathetic neuron projection extension |
| X | 1990845 | biological_process | adaptive thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA X 101 |
| Chain | Residue |
| X | SER18 |
| X | GLU21 |
| X | ASP23 |
| X | LYS26 |
| X | GLU31 |
| X | HOH226 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA X 102 |
| Chain | Residue |
| X | GLU67 |
| X | GLU72 |
| X | HOH220 |
| X | ASP61 |
| X | ASP63 |
| X | ASP65 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue 5RL X 103 |
| Chain | Residue |
| X | ASP12 |
| X | CYS84 |
| X | HIS85 |
| X | PHE88 |
| X | PHE88 |
| X | HOH208 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CA X 104 |
| Chain | Residue |
| X | HOH248 |
| X | HOH248 |
| X | HOH262 |
| X | HOH262 |
| X | HOH266 |
| X | HOH266 |
| X | HOH272 |
| X | HOH272 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04271 |
| Chain | Residue | Details |
| X | HIS15 | |
| X | SER18 | |
| X | GLU21 | |
| X | ASP23 | |
| X | HIS25 | |
| X | HIS85 | |
| X | HIS90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
| Chain | Residue | Details |
| X | ASP61 | |
| X | ASP63 | |
| X | ASP65 | |
| X | GLU67 | |
| X | GLU72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:4026304 |
| Chain | Residue | Details |
| X | SER1 |
