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 | NO2503 |
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 | NO2503 |
B | HIS306 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO2 A 503 |
Chain | Residue |
A | HIS100 |
A | HIS135 |
A | CU502 |
B | HIS306 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 501 |
Chain | Residue |
B | HIS95 |
B | CYS136 |
B | HIS145 |
B | MET150 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 502 |
Chain | Residue |
B | HIS100 |
B | HIS135 |
B | NO2503 |
C | HIS306 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO2 B 503 |
Chain | Residue |
B | HIS100 |
B | HIS135 |
B | CU502 |
C | HIS306 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU C 501 |
Chain | Residue |
C | HIS95 |
C | CYS136 |
C | HIS145 |
C | MET150 |
site_id | AD1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU C 502 |
Chain | Residue |
A | HIS306 |
C | HIS100 |
C | HIS135 |
C | NO2503 |
site_id | AD2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO2 C 503 |
Chain | Residue |
A | HIS306 |
C | HIS100 |
C | HIS135 |
C | CU502 |
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 | NO2503 |
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 |
C | NO2503 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: type 1 copper site |
Chain | Residue | Details |
A | HIS95 | |
C | CYS136 | |
C | HIS145 | |
C | MET150 | |
A | CYS136 | |
A | HIS145 | |
A | MET150 | |
B | HIS95 | |
B | CYS136 | |
B | HIS145 | |
B | MET150 | |
C | HIS95 | |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: type 2 copper site |
Chain | Residue | Details |
A | HIS100 | |
A | HIS135 | |
A | HIS306 | |
B | HIS100 | |
B | HIS135 | |
B | HIS306 | |
C | HIS100 | |
C | HIS135 | |
C | HIS306 | |
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 | |