Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0020037 | molecular_function | heme binding |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
A | 0050418 | molecular_function | hydroxylamine reductase activity |
A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0020037 | molecular_function | heme binding |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
B | 0050418 | molecular_function | hydroxylamine reductase activity |
B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM A 601 |
Chain | Residue |
A | GLY78 |
A | LYS79 |
A | LEU81 |
A | TYR93 |
A | PHE97 |
A | SER102 |
A | ALA104 |
A | GLY105 |
A | MET106 |
A | TRP109 |
A | ARG64 |
A | CYS65 |
A | CYS68 |
A | HIS69 |
A | THR77 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE DHE A 602 |
Chain | Residue |
A | ARG174 |
A | HIS200 |
A | ILE201 |
A | ARG203 |
A | ARG216 |
A | ARG243 |
A | SER244 |
A | TYR263 |
A | ALA302 |
A | ILE303 |
A | HIS345 |
A | ARG391 |
A | PHE444 |
A | GLN507 |
A | THR554 |
A | PHE557 |
A | SO2603 |
A | HOH613 |
A | HOH622 |
A | HOH641 |
A | HOH644 |
A | HOH734 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO2 A 603 |
Chain | Residue |
A | HIS345 |
A | HIS388 |
A | PHE444 |
A | DHE602 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEM B 601 |
Chain | Residue |
B | ARG64 |
B | CYS65 |
B | CYS68 |
B | HIS69 |
B | GLY78 |
B | LYS79 |
B | TYR93 |
B | SER102 |
B | ALA104 |
B | MET106 |
B | PRO107 |
B | TRP109 |
B | HOH880 |
site_id | AC5 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE DHE B 602 |
Chain | Residue |
B | PRO27 |
B | SER28 |
B | ARG174 |
B | HIS200 |
B | ILE201 |
B | ARG203 |
B | ARG216 |
B | ARG243 |
B | SER244 |
B | TYR263 |
B | ALA302 |
B | ILE303 |
B | HIS345 |
B | ARG391 |
B | PHE444 |
B | GLN507 |
B | THR554 |
B | GLY555 |
B | PHE557 |
B | SO2603 |
B | HOH604 |
B | HOH623 |
B | HOH633 |
B | HOH636 |
B | HOH637 |
B | HOH715 |
B | HOH746 |
B | HOH850 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO2 B 603 |
Chain | Residue |
B | HIS345 |
B | HIS388 |
B | PHE444 |
B | DHE602 |
site_id | C1A |
Number of Residues | 1 |
Details | THE C HEM IS THE POINT OF ELECTRON ENTRY. |
site_id | C1B |
Number of Residues | 1 |
Details | THE C HEM IS THE POINT OF ELECTRON ENTRY. |
site_id | D1A |
Number of Residues | 1 |
Details | THE D HEM IS THE SITE OF CATALYTIC ACTIVITY. |
site_id | D1B |
Number of Residues | 1 |
Details | THE D HEM IS THE SITE OF CATALYTIC ACTIVITY. |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS17 | |
A | TYR25 | |
A | HIS69 | |
A | HIS200 | |
B | HIS17 | |
B | TYR25 | |
B | HIS69 | |
B | HIS200 | |
Chain | Residue | Details |
A | SER28 | |
A | ARG391 | |
A | GLN507 | |
A | THR554 | |
B | SER28 | |
B | LYS79 | |
B | TYR93 | |
B | TRP109 | |
B | ARG174 | |
B | ARG203 | |
B | ARG216 | |
A | LYS79 | |
B | ARG243 | |
B | TYR263 | |
B | ARG391 | |
B | GLN507 | |
B | THR554 | |
A | TYR93 | |
A | TRP109 | |
A | ARG174 | |
A | ARG203 | |
A | ARG216 | |
A | ARG243 | |
A | TYR263 | |
Chain | Residue | Details |
A | CYS65 | |
A | CYS68 | |
B | CYS65 | |
B | CYS68 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nir |
Chain | Residue | Details |
A | HIS388 | |
A | HIS345 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nir |
Chain | Residue | Details |
B | HIS388 | |
B | HIS345 | |