5XM5
Crystal structure of Zinc binding protein ZinT at 1.49 Angstrom from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006882 | biological_process | intracellular zinc ion homeostasis |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0034224 | biological_process | cellular response to zinc ion starvation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046870 | molecular_function | cadmium ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070301 | biological_process | cellular response to hydrogen peroxide |
| A | 0071276 | biological_process | cellular response to cadmium ion |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006882 | biological_process | intracellular zinc ion homeostasis |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0034224 | biological_process | cellular response to zinc ion starvation |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046870 | molecular_function | cadmium ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070301 | biological_process | cellular response to hydrogen peroxide |
| B | 0071276 | biological_process | cellular response to cadmium ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 201 |
| Chain | Residue |
| A | ALA59 |
| A | ASP62 |
| A | LYS65 |
| A | HOH430 |
| A | HOH494 |
| A | HOH502 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 202 |
| Chain | Residue |
| A | HIS193 |
| A | SER152 |
| A | HIS153 |
| A | GLU189 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 203 |
| Chain | Residue |
| A | HIS144 |
| A | HIS153 |
| A | HIS155 |
| A | NA206 |
| A | HOH460 |
| A | HOH480 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 204 |
| Chain | Residue |
| A | THR101 |
| A | SER102 |
| A | LYS134 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 205 |
| Chain | Residue |
| A | ILE82 |
| A | ARG96 |
| A | PRO136 |
| A | MET158 |
| A | HOH508 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 206 |
| Chain | Residue |
| A | HIS144 |
| A | HIS155 |
| A | ZN203 |
| A | HOH460 |
| A | HOH480 |
| A | HOH556 |
| A | HOH564 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 201 |
| Chain | Residue |
| B | HIS144 |
| B | HIS153 |
| B | HIS155 |
| B | HOH385 |
| B | HOH417 |
| B | HOH457 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 202 |
| Chain | Residue |
| A | HOH488 |
| B | ALA59 |
| B | ASP62 |
| B | LYS65 |
| B | HOH435 |
| B | HOH458 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 203 |
| Chain | Residue |
| B | SER152 |
| B | HIS153 |
| B | GLU189 |
| B | HIS193 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 204 |
| Chain | Residue |
| B | HOH385 |
| B | HOH403 |
| B | HOH504 |
| B | HOH516 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue NA B 205 |
| Chain | Residue |
| B | THR80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10, ECO:0000269|Ref.11 |
| Chain | Residue | Details |
| A | HIS144 | |
| B | HIS193 | |
| A | HIS153 | |
| A | HIS155 | |
| A | GLU189 | |
| A | HIS193 | |
| B | HIS144 | |
| B | HIS153 | |
| B | HIS155 | |
| B | GLU189 |
