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 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 502 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | NO2503 |
| B | HIS306 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO2 A 503 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | CU502 |
| A | HOH650 |
| B | HIS255 |
| B | ILE257 |
| B | HIS306 |
| B | LEU308 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 501 |
| Chain | Residue |
| B | HIS95 |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 502 |
| Chain | Residue |
| B | ASP98 |
| B | HIS100 |
| B | HIS135 |
| B | NO2503 |
| C | HIS306 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO2 B 503 |
| Chain | Residue |
| B | ASP98 |
| B | HIS100 |
| B | HIS135 |
| B | CU502 |
| B | HOH649 |
| C | HIS255 |
| C | ILE257 |
| C | HIS306 |
| C | LEU308 |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 502 |
| Chain | Residue |
| A | HIS306 |
| C | ASP98 |
| C | HIS100 |
| C | HIS135 |
| C | NO2503 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO2 C 503 |
| Chain | Residue |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| A | LEU308 |
| C | ASP98 |
| C | HIS100 |
| C | HIS135 |
| C | CU502 |
| C | HOH656 |
| site_id | CU1 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | CU2 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| B | HIS306 |
| A | NO2503 |
| site_id | CU3 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| B | HIS95 |
| site_id | CU4 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| C | HIS306 |
| B | NO2503 |
| site_id | CU5 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | CU6 |
| Number of Residues | 4 |
| Details | COPPER SITE. |
| Chain | Residue |
| C | HIS100 |
| C | HIS135 |
| A | HIS306 |
| C | NO2503 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"type 2 copper site"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"type 1 copper site"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]} |
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 | |
