3CZT
Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0001726 | cellular_component | ruffle |
| 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 | 0005654 | cellular_component | nucleoplasm |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0005829 | cellular_component | cytosol |
| X | 0007155 | biological_process | cell adhesion |
| X | 0007409 | biological_process | axonogenesis |
| X | 0007417 | biological_process | central nervous system development |
| X | 0007611 | biological_process | learning or memory |
| X | 0007613 | biological_process | memory |
| X | 0008270 | molecular_function | zinc ion binding |
| X | 0008284 | biological_process | positive regulation of cell population proliferation |
| X | 0042802 | molecular_function | identical protein binding |
| X | 0042803 | molecular_function | protein homodimerization activity |
| X | 0043025 | cellular_component | neuronal cell body |
| X | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| X | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| X | 0044548 | molecular_function | S100 protein binding |
| X | 0045666 | biological_process | positive regulation of neuron differentiation |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0048156 | molecular_function | tau protein binding |
| X | 0048168 | biological_process | regulation of neuronal synaptic plasticity |
| X | 0048306 | molecular_function | calcium-dependent protein binding |
| X | 0048471 | cellular_component | perinuclear region of cytoplasm |
| X | 0050786 | molecular_function | RAGE receptor binding |
| X | 0097490 | biological_process | sympathetic neuron projection extension |
| X | 1990138 | biological_process | 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 92 |
| Chain | Residue |
| X | SER18 |
| X | GLU21 |
| X | ASP23 |
| X | LYS26 |
| X | GLU31 |
| X | HOH120 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA X 93 |
| Chain | Residue |
| X | GLU67 |
| X | GLU72 |
| X | HOH104 |
| X | ASP61 |
| X | ASP63 |
| X | ASP65 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA X 94 |
| Chain | Residue |
| X | HOH126 |
| X | HOH135 |
| X | HOH161 |
| X | HOH187 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN X 95 |
| Chain | Residue |
| X | HIS15 |
| X | HIS25 |
| X | HIS85 |
| X | HIS90 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA X 92 |
| Chain | Residue |
| X | SER18 |
| X | GLU21 |
| X | ASP23 |
| X | LYS26 |
| X | GLU31 |
| X | HOH120 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA X 93 |
| Chain | Residue |
| X | ASP61 |
| X | ASP63 |
| X | ASP65 |
| X | GLU67 |
| X | GLU72 |
| X | HOH104 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CA X 94 |
| Chain | Residue |
| X | HOH126 |
| X | HOH126 |
| X | HOH135 |
| X | HOH135 |
| X | HOH161 |
| X | HOH161 |
| X | HOH187 |
| X | HOH187 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN X 95 |
| Chain | Residue |
| X | HIS15 |
| X | HIS25 |
| X | HIS85 |
| X | HIS90 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT |
| Chain | Residue | Details |
| X | HIS15 | |
| X | HIS25 | |
| X | HIS85 | |
| X | HIS90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10 |
| Chain | Residue | Details |
| X | SER18 | |
| X | GLU21 | |
| X | ASP23 | |
| X | LYS26 | |
| X | GLU31 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10 |
| Chain | Residue | Details |
| X | ASP61 | |
| X | ASP65 | |
| X | GLU67 | |
| X | GLU72 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:2H61, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10 |
| Chain | Residue | Details |
| X | ASP63 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638 |
| Chain | Residue | Details |
| X | SER1 |
