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 | MONOMER A TYPE 1 COPPER SITE. |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | MONOMER A TYPE 2 COPPER SITE. |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | HIS306 |
| A | HOH503 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 502 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | HOH503 |
| B | HIS306 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 501 |
| Chain | Residue |
| B | HIS95 |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 502 |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| B | HOH503 |
| C | HIS306 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 501 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 502 |
| Chain | Residue |
| A | HIS306 |
| A | HOH504 |
| C | HIS100 |
| C | HIS135 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | MONOMER B TYPE 1 COPPER SITE. |
| Chain | Residue |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| B | HIS95 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | MONOMER B TYPE 2 COPPER SITE. |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| B | HIS306 |
| B | HOH503 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | MONOMER C TYPE 1 COPPER SITE. |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | MONOMER C TYPE 2 COPPER SITE. |
| Chain | Residue |
| C | HIS100 |
| C | HIS135 |
| C | HIS306 |
| A | HOH504 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 492 |
| Details | Domain: {"description":"Plastocyanin-like 1"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 492 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"type 1 copper site"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"type 2 copper site"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | PHE64 | |
| A | GLY66 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | PHE64 | |
| B | GLY66 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | PHE64 | |
| C | GLY66 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | ASP98 | |
| A | HIS255 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | ASP98 | |
| B | HIS255 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | ASP98 | |
| C | HIS255 | |
