Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019333 | biological_process | denitrification pathway |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019333 | biological_process | denitrification pathway |
| B | 0042128 | biological_process | nitrate assimilation |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019333 | biological_process | denitrification pathway |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 401 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CU A 402 |
| Chain | Residue |
| C | HOH842 |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HOH505 |
| C | HIS306 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue MPD A 403 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MPD A 404 |
| Chain | Residue |
| A | ALA10 |
| A | ARG14 |
| B | HOH506 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue ACY A 405 |
| Chain | Residue |
| A | GLY140 |
| A | MET141 |
| A | VAL142 |
| A | PRO143 |
| A | TRP144 |
| A | TYR203 |
| C | GLU313 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CU A 406 |
| Chain | Residue |
| A | HIS306 |
| A | HOH718 |
| B | ASP98 |
| B | HIS100 |
| B | HIS135 |
| B | HOH509 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 401 |
| Chain | Residue |
| B | HIS95 |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MPD B 402 |
| Chain | Residue |
| A | PHE312 |
| B | PRO139 |
| B | HOH526 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue ACY B 403 |
| Chain | Residue |
| A | GLU313 |
| B | GLY140 |
| B | MET141 |
| B | VAL142 |
| B | PRO143 |
| B | TRP144 |
| B | TYR203 |
| B | MET210 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue ACY B 404 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CU B 405 |
| Chain | Residue |
| B | HIS306 |
| B | HOH746 |
| C | ASP98 |
| C | HIS100 |
| C | HIS135 |
| C | HOH602 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue MPD C 501 |
| Chain | Residue |
| A | LEU106 |
| A | ALA137 |
| A | PRO139 |
| C | ILE300 |
| C | ALA302 |
| C | PHE312 |
| C | HOH625 |
| C | HOH668 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CU C 502 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MPD C 503 |
| Chain | Residue |
| B | ILE300 |
| C | LEU106 |
| C | PRO139 |
| C | HOH611 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue MPD C 504 |
| Chain | Residue |
| C | GLU46 |
| C | HOH866 |
| C | HOH900 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue ACY C 505 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue ACY C 506 |
| Chain | Residue |
| C | HIS28 |
| C | GLN30 |
| C | HOH774 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 492 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"type 2 copper site"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"type 1 copper site"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]} |
