4PE7
Crystal Structure of Calcium-loaded S100B bound to SC1982
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006417 | biological_process | regulation of translation |
A | 0007155 | biological_process | cell adhesion |
A | 0007409 | biological_process | axonogenesis |
A | 0007611 | biological_process | learning or memory |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008284 | biological_process | positive regulation of cell population proliferation |
A | 0016310 | biological_process | phosphorylation |
A | 0019210 | molecular_function | kinase inhibitor activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
A | 0044548 | molecular_function | S100 protein binding |
A | 0045917 | biological_process | positive regulation of complement activation |
A | 0046872 | molecular_function | metal ion binding |
A | 0048143 | biological_process | astrocyte activation |
A | 0048156 | molecular_function | tau protein binding |
A | 0048306 | molecular_function | calcium-dependent protein binding |
A | 0050786 | molecular_function | RAGE receptor binding |
A | 0071638 | biological_process | negative regulation of monocyte chemotactic protein-1 production |
A | 0097490 | biological_process | sympathetic neuron projection extension |
A | 1990845 | biological_process | adaptive thermogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ODN A 101 |
Chain | Residue |
A | MET0 |
A | HIS42 |
A | HIS42 |
A | PHE43 |
A | CYS84 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 102 |
Chain | Residue |
A | GLU31 |
A | HOH299 |
A | SER18 |
A | GLU21 |
A | ASP23 |
A | LYS26 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 103 |
Chain | Residue |
A | ASP61 |
A | ASP63 |
A | ASP65 |
A | GLU67 |
A | GLU72 |
A | HOH296 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue CA A 104 |
Chain | Residue |
A | ASP63 |
A | ASP69 |
A | HOH208 |
A | HOH214 |
A | HOH216 |
A | HOH246 |
A | HOH278 |
A | HOH283 |
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 |
A | HIS15 | |
A | SER18 | |
A | GLU21 | |
A | ASP23 | |
A | HIS25 | |
A | HIS85 | |
A | HIS90 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
A | ASP61 | |
A | ASP63 | |
A | ASP65 | |
A | GLU67 | |
A | GLU72 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:4026304 |
Chain | Residue | Details |
A | SER1 |