Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019645 | biological_process | anaerobic electron transport chain |
A | 0020037 | molecular_function | heme binding |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042128 | biological_process | nitrate assimilation |
A | 0042279 | molecular_function | nitrite reductase (cytochrome, ammonia-forming) activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
B | 0005506 | molecular_function | iron ion binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019645 | biological_process | anaerobic electron transport chain |
B | 0020037 | molecular_function | heme binding |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042128 | biological_process | nitrate assimilation |
B | 0042279 | molecular_function | nitrite reductase (cytochrome, ammonia-forming) activity |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEC A 471 |
Chain | Residue |
A | LYS86 |
A | TYR206 |
A | PHE208 |
A | HIS257 |
A | HIS381 |
A | HEC473 |
A | HOH488 |
A | HOH516 |
A | HOH519 |
A | HOH531 |
A | HOH539 |
A | ASP97 |
A | THR101 |
A | ARG103 |
A | CYS119 |
A | CYS122 |
A | LYS123 |
A | CYS202 |
A | HIS203 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HEC A 472 |
Chain | Residue |
A | PHE46 |
A | GLN49 |
A | GLY156 |
A | CYS157 |
A | CYS160 |
A | HIS161 |
A | PRO166 |
A | VAL276 |
A | MET280 |
A | THR292 |
A | HIS294 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEC A 473 |
Chain | Residue |
A | SER59 |
A | PRO88 |
A | ARG89 |
A | HIS91 |
A | TYR93 |
A | ALA94 |
A | ASP97 |
A | CYS122 |
A | LYS123 |
A | ILE155 |
A | ASP159 |
A | ARG172 |
A | VAL198 |
A | CYS199 |
A | CYS202 |
A | HIS203 |
A | HIS279 |
A | VAL296 |
A | GLY297 |
A | HEC471 |
A | HEC474 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEC A 474 |
Chain | Residue |
A | PRO88 |
A | HIS203 |
A | GLU259 |
A | TRP263 |
A | HIS268 |
A | VAL273 |
A | SER274 |
A | CYS275 |
A | CYS278 |
A | HIS279 |
A | PRO299 |
A | LYS326 |
A | HIS381 |
A | GLY382 |
A | ALA385 |
A | HIS386 |
A | HEC473 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEC A 475 |
Chain | Residue |
A | ILE267 |
A | HIS268 |
A | ASN271 |
A | VAL273 |
A | PRO299 |
A | PHE300 |
A | THR306 |
A | CYS307 |
A | CYS310 |
A | HIS311 |
A | ARG325 |
B | HIS311 |
B | GLN313 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 476 |
Chain | Residue |
A | GLU205 |
A | TYR206 |
A | TYR235 |
A | LYS254 |
A | GLN256 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEC B 471 |
Chain | Residue |
B | HIS257 |
B | HEC473 |
B | HOH484 |
B | HOH488 |
B | HOH499 |
B | LYS86 |
B | PRO88 |
B | ASP97 |
B | THR101 |
B | ARG103 |
B | LEU115 |
B | CYS119 |
B | CYS122 |
B | LYS123 |
B | CYS202 |
B | HIS203 |
B | TYR206 |
B | PHE208 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEC B 472 |
Chain | Residue |
B | PHE46 |
B | GLN49 |
B | TYR50 |
B | GLY156 |
B | CYS157 |
B | CYS160 |
B | HIS161 |
B | PRO166 |
B | MET280 |
B | LYS282 |
B | THR292 |
B | HIS294 |
site_id | AC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEC B 473 |
Chain | Residue |
B | SER59 |
B | PRO88 |
B | ARG89 |
B | GLY90 |
B | HIS91 |
B | TYR93 |
B | ALA94 |
B | ASP97 |
B | CYS122 |
B | ILE155 |
B | VAL198 |
B | CYS199 |
B | GLN201 |
B | CYS202 |
B | HIS203 |
B | HIS279 |
B | MET280 |
B | VAL296 |
B | HEC471 |
B | HEC474 |
site_id | BC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEC B 474 |
Chain | Residue |
B | HIS203 |
B | GLU259 |
B | TRP263 |
B | HIS268 |
B | VAL273 |
B | SER274 |
B | CYS275 |
B | CYS278 |
B | HIS279 |
B | ASN298 |
B | PRO299 |
B | LYS326 |
B | GLY382 |
B | ALA385 |
B | HIS386 |
B | HEC473 |
B | HEC475 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEC B 475 |
Chain | Residue |
A | HIS311 |
A | GLN313 |
B | ILE267 |
B | HIS268 |
B | ASN271 |
B | VAL273 |
B | PHE300 |
B | THR306 |
B | CYS307 |
B | CYS310 |
B | HIS311 |
B | ARG325 |
B | HEC474 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 476 |
Chain | Residue |
B | GLU205 |
B | TYR206 |
B | LYS254 |
B | GLN256 |
B | HOH483 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS91 | |
B | HIS91 | |
B | LYS123 | |
B | HIS161 | |
B | HIS203 | |
B | HIS268 | |
B | HIS279 | |
B | HIS294 | |
B | HIS311 | |
B | HIS386 | |
A | LYS123 | |
A | HIS161 | |
A | HIS203 | |
A | HIS268 | |
A | HIS279 | |
A | HIS294 | |
A | HIS311 | |
A | HIS386 | |
Chain | Residue | Details |
A | CYS119 | |
B | CYS307 | |
A | CYS199 | |
A | CYS202 | |
A | CYS275 | |
A | CYS307 | |
B | CYS119 | |
B | CYS199 | |
B | CYS202 | |
B | CYS275 | |
Chain | Residue | Details |
A | CYS122 | |
B | CYS122 | |
Chain | Residue | Details |
A | CYS157 | |
A | CYS160 | |
A | CYS278 | |
A | CYS310 | |
B | CYS157 | |
B | CYS160 | |
B | CYS278 | |
B | CYS310 | |
Chain | Residue | Details |
A | GLU205 | |
A | LYS254 | |
A | GLN256 | |
B | GLU205 | |
B | LYS254 | |
B | GLN256 | |
Chain | Residue | Details |
A | TYR206 | |
A | HIS257 | |
B | TYR206 | |
B | HIS257 | |