3UBR
Laue structure of Shewanella oneidensis cytochrome-c Nitrite Reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0009061 | biological_process | anaerobic respiration |
| 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 | 0009061 | biological_process | anaerobic respiration |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3UBR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3UBR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3UBR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01182","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
