Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0019333 | biological_process | denitrification pathway |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0019333 | biological_process | denitrification pathway |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0019333 | biological_process | denitrification pathway |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 345 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 346 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| B | HIS306 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 345 |
| Chain | Residue |
| B | HIS145 |
| B | MET150 |
| B | HIS95 |
| B | CYS136 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU B 346 |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| C | HIS306 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 345 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU C 346 |
| Chain | Residue |
| A | HIS306 |
| C | HIS100 |
| C | HIS135 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 124 |
| Chain | Residue |
| D | HIS40 |
| D | CYS78 |
| D | HIS81 |
| D | MET86 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GD A 347 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GD C 347 |
Functional Information from PROSITE/UniProt
| site_id | PS00196 |
| Number of Residues | 15 |
| Details | COPPER_BLUE Type-1 copper (blue) proteins signature. Ga.YlVKCt.P.HyamgM |
| Chain | Residue | Details |
| D | GLY72-MET86 | |
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"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 88 |
| Details | Domain: {"description":"Plastocyanin-like"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2909547","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 | ASP98 | |
| A | HIS255 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | ASP98 | |
| B | HIS255 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | ASP98 | |
| C | HIS255 | |