3TOR
Crystal structure of Escherichia coli NrfA with Europium bound
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 | 0016966 | molecular_function | nitric oxide reductase 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 | 0016966 | molecular_function | nitric oxide reductase 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 |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0009061 | biological_process | anaerobic respiration |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016966 | molecular_function | nitric oxide reductase activity |
| C | 0019645 | biological_process | anaerobic electron transport chain |
| C | 0020037 | molecular_function | heme binding |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0042279 | molecular_function | nitrite reductase (cytochrome, ammonia-forming) activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0009061 | biological_process | anaerobic respiration |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016966 | molecular_function | nitric oxide reductase activity |
| D | 0019645 | biological_process | anaerobic electron transport chain |
| D | 0020037 | molecular_function | heme binding |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0042128 | biological_process | nitrate assimilation |
| D | 0042279 | molecular_function | nitrite reductase (cytochrome, ammonia-forming) activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1 |
| Chain | Residue |
| A | HOH21 |
| A | GLU215 |
| A | TYR216 |
| A | LYS261 |
| A | GLN263 |
| A | HOH583 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EU A 2 |
| Chain | Residue |
| A | HOH525 |
| A | HOH626 |
| A | HOH825 |
| A | HOH854 |
| A | HOH1993 |
| A | HEC5 |
| A | HEC6 |
| A | PRO91 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 3 |
| Chain | Residue |
| A | HEC5 |
| A | HOH10 |
| A | HOH13 |
| A | HOH24 |
| A | TYR88 |
| A | ASN89 |
| A | PRO91 |
| A | ASP100 |
| A | THR104 |
| A | ARG106 |
| A | CYS122 |
| A | CYS125 |
| A | LYS126 |
| A | CYS212 |
| A | HIS213 |
| A | TYR216 |
| A | HIS264 |
| A | HIS388 |
| A | HOH487 |
| A | HOH502 |
| A | HOH518 |
| A | HOH537 |
| A | HOH577 |
| A | HOH1316 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC A 4 |
| Chain | Residue |
| A | HEC5 |
| A | HIS49 |
| A | GLN52 |
| A | TYR53 |
| A | TRP56 |
| A | GLY159 |
| A | CYS160 |
| A | CYS163 |
| A | HIS164 |
| A | PHE171 |
| A | GLY174 |
| A | ARG201 |
| A | GLN205 |
| A | ILE283 |
| A | MET287 |
| A | LYS289 |
| A | TYR298 |
| A | THR299 |
| A | HIS301 |
| A | ILE303 |
| A | HOH544 |
| A | HOH634 |
| A | HOH1049 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HEC A 5 |
| Chain | Residue |
| A | EU2 |
| A | HEC3 |
| A | HEC4 |
| A | HEC6 |
| A | GLN62 |
| A | PRO91 |
| A | ARG92 |
| A | GLY93 |
| A | HIS94 |
| A | PHE96 |
| A | ALA97 |
| A | ASP100 |
| A | CYS125 |
| A | LYS126 |
| A | LEU158 |
| A | ARG182 |
| A | VAL208 |
| A | CYS209 |
| A | CYS212 |
| A | HIS213 |
| A | ILE283 |
| A | HIS286 |
| A | MET287 |
| A | ILE303 |
| A | GLY304 |
| A | HOH620 |
| A | HOH626 |
| A | HOH854 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEC A 6 |
| Chain | Residue |
| A | CYS282 |
| A | CYS285 |
| A | HIS286 |
| A | PRO306 |
| A | PHE307 |
| A | HIS388 |
| A | HIS391 |
| A | MET392 |
| A | HIS393 |
| A | HOH596 |
| A | HOH724 |
| A | HOH825 |
| A | HOH843 |
| A | HOH854 |
| A | HOH1189 |
| A | EU2 |
| A | HEC5 |
| A | HEC7 |
| A | PRO91 |
| A | HIS213 |
| A | GLU266 |
| A | TRP270 |
| A | HIS275 |
| A | VAL280 |
| A | THR281 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC A 7 |
| Chain | Residue |
| A | HEC6 |
| A | HIS275 |
| A | VAL280 |
| A | ASP284 |
| A | PRO306 |
| A | PHE307 |
| A | THR313 |
| A | CYS314 |
| A | CYS317 |
| A | HIS318 |
| A | ARG332 |
| A | MET392 |
| A | EU479 |
| A | EU480 |
| A | HOH534 |
| A | HOH897 |
| D | HEC7 |
| D | HIS318 |
| D | GLN320 |
| D | GLU396 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EU A 479 |
| Chain | Residue |
| A | HEC7 |
| A | HOH1459 |
| D | HEC7 |
| D | HOH652 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EU A 480 |
| Chain | Residue |
| A | HEC7 |
| A | GLU396 |
| D | HEC7 |
| D | GLU396 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1 |
| Chain | Residue |
| B | GLU215 |
| B | TYR216 |
| B | LYS261 |
| B | GLN263 |
| B | HOH566 |
| B | HOH635 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EU B 2 |
| Chain | Residue |
| B | HEC5 |
| B | HEC6 |
| B | PRO91 |
| B | HOH541 |
| B | HOH562 |
| B | HOH686 |
| B | HOH690 |
| B | HOH1976 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC B 3 |
| Chain | Residue |
| B | HEC5 |
| B | HOH11 |
| B | HOH22 |
| B | TYR88 |
| B | ASN89 |
| B | PRO91 |
| B | ASP100 |
| B | THR104 |
| B | ARG106 |
| B | THR107 |
| B | CYS122 |
| B | CYS125 |
| B | LYS126 |
| B | CYS212 |
| B | HIS213 |
| B | TYR216 |
| B | PHE218 |
| B | HIS264 |
| B | HIS388 |
| B | HOH495 |
| B | HOH504 |
| B | HOH509 |
| B | HOH527 |
| B | HOH533 |
| B | HOH557 |
| B | HOH829 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC B 4 |
| Chain | Residue |
| B | HEC5 |
| B | HIS49 |
| B | GLN52 |
| B | TYR53 |
| B | TRP56 |
| B | GLY159 |
| B | CYS160 |
| B | CYS163 |
| B | HIS164 |
| B | PHE171 |
| B | GLY174 |
| B | ARG201 |
| B | GLN205 |
| B | ILE283 |
| B | MET287 |
| B | LYS289 |
| B | TYR298 |
| B | THR299 |
| B | HIS301 |
| B | HOH529 |
| B | HOH570 |
| B | HOH1105 |
| site_id | BC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HEC B 5 |
| Chain | Residue |
| B | EU2 |
| B | HEC3 |
| B | HEC4 |
| B | HEC6 |
| B | GLN62 |
| B | PRO91 |
| B | ARG92 |
| B | GLY93 |
| B | HIS94 |
| B | PHE96 |
| B | ALA97 |
| B | ASP100 |
| B | CYS125 |
| B | LYS126 |
| B | LEU158 |
| B | ARG182 |
| B | VAL208 |
| B | CYS209 |
| B | CYS212 |
| B | HIS213 |
| B | ILE283 |
| B | HIS286 |
| B | MET287 |
| B | ILE303 |
| B | GLY304 |
| B | HOH562 |
| B | HOH567 |
| B | HOH690 |
| B | HOH1350 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC B 6 |
| Chain | Residue |
| B | EU2 |
| B | HEC5 |
| B | HEC7 |
| B | PRO91 |
| B | HIS213 |
| B | GLU266 |
| B | TRP270 |
| B | HIS275 |
| B | VAL280 |
| B | THR281 |
| B | CYS282 |
| B | CYS285 |
| B | HIS286 |
| B | ASN305 |
| B | PRO306 |
| B | PHE307 |
| B | HIS388 |
| B | HIS391 |
| B | MET392 |
| B | HIS393 |
| B | HOH492 |
| B | HOH686 |
| B | HOH687 |
| B | HOH690 |
| B | HOH823 |
| B | HOH1433 |
| site_id | BC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B 7 |
| Chain | Residue |
| B | HEC6 |
| B | ILE274 |
| B | HIS275 |
| B | VAL280 |
| B | ASP284 |
| B | PRO306 |
| B | PHE307 |
| B | THR313 |
| B | CYS314 |
| B | CYS317 |
| B | HIS318 |
| B | ARG332 |
| B | MET392 |
| B | EU479 |
| B | EU480 |
| B | HOH644 |
| B | HOH992 |
| C | HEC7 |
| C | HIS318 |
| C | GLN320 |
| C | GLU396 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EU B 479 |
| Chain | Residue |
| B | HEC7 |
| B | HOH1718 |
| C | HEC7 |
| C | HOH611 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EU B 480 |
| Chain | Residue |
| B | HEC7 |
| B | GLU396 |
| C | HEC7 |
| C | GLU396 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 1 |
| Chain | Residue |
| C | GLU215 |
| C | TYR216 |
| C | LYS261 |
| C | GLN263 |
| C | HOH509 |
| C | HOH583 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EU C 2 |
| Chain | Residue |
| C | HEC5 |
| C | HEC6 |
| C | PRO91 |
| C | HOH645 |
| C | HOH858 |
| C | HOH1356 |
| C | HOH1509 |
| C | HOH1793 |
| site_id | CC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC C 3 |
| Chain | Residue |
| C | HEC5 |
| C | TYR88 |
| C | ASN89 |
| C | PRO91 |
| C | ASP100 |
| C | THR104 |
| C | ARG106 |
| C | THR107 |
| C | LEU118 |
| C | CYS122 |
| C | CYS125 |
| C | LYS126 |
| C | CYS212 |
| C | HIS213 |
| C | TYR216 |
| C | HIS264 |
| C | HIS388 |
| C | HOH486 |
| C | HOH488 |
| C | HOH500 |
| C | HOH505 |
| C | HOH514 |
| C | HOH515 |
| C | HOH537 |
| C | HOH634 |
| C | HOH1045 |
| site_id | CC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC C 4 |
| Chain | Residue |
| C | HEC5 |
| C | HIS49 |
| C | GLN52 |
| C | TRP56 |
| C | GLY159 |
| C | CYS160 |
| C | CYS163 |
| C | HIS164 |
| C | PHE171 |
| C | GLY174 |
| C | PRO176 |
| C | LEU178 |
| C | ARG201 |
| C | GLN205 |
| C | ILE283 |
| C | LYS289 |
| C | TYR298 |
| C | THR299 |
| C | HIS301 |
| C | HOH539 |
| C | HOH1720 |
| site_id | CC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC C 5 |
| Chain | Residue |
| C | EU2 |
| C | HEC3 |
| C | HEC4 |
| C | HEC6 |
| C | GLN62 |
| C | PRO91 |
| C | ARG92 |
| C | GLY93 |
| C | HIS94 |
| C | PHE96 |
| C | ALA97 |
| C | ASP100 |
| C | CYS125 |
| C | LYS126 |
| C | LEU158 |
| C | VAL208 |
| C | CYS209 |
| C | CYS212 |
| C | HIS213 |
| C | ILE283 |
| C | HIS286 |
| C | MET287 |
| C | ILE303 |
| C | HOH1509 |
| site_id | CC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEC C 6 |
| Chain | Residue |
| C | EU2 |
| C | HEC5 |
| C | HEC7 |
| C | PRO91 |
| C | HIS213 |
| C | GLU266 |
| C | TRP270 |
| C | HIS275 |
| C | VAL280 |
| C | THR281 |
| C | CYS282 |
| C | CYS285 |
| C | HIS286 |
| C | ASN305 |
| C | PRO306 |
| C | PHE307 |
| C | HIS388 |
| C | GLY389 |
| C | HIS391 |
| C | MET392 |
| C | HIS393 |
| C | HOH693 |
| C | HOH835 |
| C | HOH1183 |
| C | HOH1356 |
| site_id | CC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC C 7 |
| Chain | Residue |
| B | HEC7 |
| B | ILE274 |
| B | HIS318 |
| B | GLN320 |
| B | GLU396 |
| B | EU479 |
| B | EU480 |
| C | HEC6 |
| C | ILE274 |
| C | HIS275 |
| C | VAL280 |
| C | ASP284 |
| C | PHE307 |
| C | THR313 |
| C | CYS314 |
| C | CYS317 |
| C | HIS318 |
| C | ARG332 |
| C | MET392 |
| C | HOH961 |
| C | HOH969 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EU C 479 |
| Chain | Residue |
| A | ASP457 |
| A | HOH826 |
| A | HOH1514 |
| C | GLU190 |
| C | HOH521 |
| C | HOH622 |
| C | HOH866 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 1 |
| Chain | Residue |
| D | GLU215 |
| D | TYR216 |
| D | LYS261 |
| D | GLN263 |
| D | HOH509 |
| D | HOH543 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EU D 2 |
| Chain | Residue |
| D | HEC5 |
| D | HEC6 |
| D | PRO91 |
| D | HOH725 |
| D | HOH783 |
| D | HOH1000 |
| D | HOH1042 |
| site_id | DC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HEC D 3 |
| Chain | Residue |
| D | HEC5 |
| D | HOH17 |
| D | TYR88 |
| D | ASN89 |
| D | PRO91 |
| D | ASP100 |
| D | THR104 |
| D | ARG106 |
| D | THR107 |
| D | LEU118 |
| D | CYS122 |
| D | CYS125 |
| D | LYS126 |
| D | CYS212 |
| D | HIS213 |
| D | TYR216 |
| D | PHE218 |
| D | VAL225 |
| D | HIS264 |
| D | HIS388 |
| D | HOH485 |
| D | HOH489 |
| D | HOH496 |
| D | HOH517 |
| D | HOH542 |
| D | HOH590 |
| D | HOH613 |
| D | HOH818 |
| site_id | DC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC D 4 |
| Chain | Residue |
| D | HEC5 |
| D | HIS49 |
| D | GLN52 |
| D | TYR53 |
| D | TRP56 |
| D | GLY159 |
| D | CYS160 |
| D | CYS163 |
| D | HIS164 |
| D | PHE171 |
| D | GLY174 |
| D | PRO176 |
| D | ARG201 |
| D | GLN205 |
| D | ILE283 |
| D | LYS289 |
| D | TYR298 |
| D | THR299 |
| D | HIS301 |
| D | HOH515 |
| D | HOH1968 |
| site_id | DC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC D 5 |
| Chain | Residue |
| D | EU2 |
| D | HEC3 |
| D | HEC4 |
| D | HEC6 |
| D | GLN62 |
| D | PRO91 |
| D | ARG92 |
| D | GLY93 |
| D | HIS94 |
| D | PHE96 |
| D | ALA97 |
| D | ASP100 |
| D | CYS125 |
| D | LEU158 |
| D | VAL208 |
| D | CYS209 |
| D | CYS212 |
| D | HIS213 |
| D | ILE283 |
| D | HIS286 |
| D | MET287 |
| D | ILE303 |
| D | HOH522 |
| D | HOH1042 |
| site_id | DC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC D 6 |
| Chain | Residue |
| D | EU2 |
| D | HEC5 |
| D | HEC7 |
| D | PRO91 |
| D | HIS213 |
| D | GLU266 |
| D | TRP270 |
| D | HIS275 |
| D | VAL280 |
| D | THR281 |
| D | CYS282 |
| D | CYS285 |
| D | HIS286 |
| D | ASN305 |
| D | PRO306 |
| D | HIS388 |
| D | HIS391 |
| D | MET392 |
| D | HIS393 |
| D | HOH725 |
| D | HOH844 |
| D | HOH1065 |
| site_id | DC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC D 7 |
| Chain | Residue |
| A | HEC7 |
| A | ILE274 |
| A | HIS318 |
| A | GLN320 |
| A | GLU396 |
| A | EU479 |
| A | EU480 |
| D | HEC6 |
| D | HIS275 |
| D | VAL280 |
| D | PHE307 |
| D | THR313 |
| D | CYS314 |
| D | CYS317 |
| D | HIS318 |
| D | ARG332 |
| D | MET392 |
| D | HOH591 |
| D | HOH1060 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PDB","id":"1GU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RF7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PDB","id":"1GU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RF7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1GU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RF7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1GU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PDB","id":"1GU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RF7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
