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 | HIS126 |
A | CYS167 |
A | HIS177 |
A | THR182 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 402 |
Chain | Residue |
A | ASP129 |
A | HIS131 |
A | HIS166 |
A | HOH3541 |
B | HIS1338 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 1401 |
Chain | Residue |
B | HIS1126 |
B | CYS1167 |
B | HIS1177 |
B | THR1182 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 1402 |
Chain | Residue |
B | HIS1131 |
B | HIS1166 |
B | HOH3542 |
C | HIS2338 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU C 2401 |
Chain | Residue |
C | HIS2126 |
C | CYS2167 |
C | HIS2177 |
C | THR2182 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU C 2402 |
Chain | Residue |
A | HIS338 |
C | ASP2129 |
C | HIS2131 |
C | HIS2166 |
C | HOH3543 |
Functional Information from PROSITE/UniProt
site_id | PS00283 |
Number of Residues | 17 |
Details | SOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LkDHEGKpVrYDtvYyI |
Chain | Residue | Details |
A | LEU194-ILE210 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 288 |
Details | Domain: {"description":"Plastocyanin-like 1"} |
site_id | SWS_FT_FI2 |
Number of Residues | 303 |
Details | Domain: {"description":"Plastocyanin-like 2"} |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"description":"type 1 copper site","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | Binding site: {"description":"type 2 copper site","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
A | GLY97 | |
A | PHE95 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
B | PHE1095 | |
B | GLY1097 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
C | GLY2097 | |
C | PHE2095 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
A | HIS287 | |
A | ASP129 | |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
B | HIS1287 | |
B | ASP1129 | |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
C | ASP2129 | |
C | HIS2287 | |