1IQC
Crystal structure of Di-Heme Peroxidase from Nitrosomonas europaea
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| 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 | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| B | 0004601 | molecular_function | peroxidase 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 | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004130 | molecular_function | cytochrome-c peroxidase activity |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 410 |
| Chain | Residue |
| A | ASN67 |
| A | THR239 |
| A | PRO241 |
| A | HOH1421 |
| A | HOH1423 |
| A | HOH1425 |
| A | HOH1426 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 1411 |
| Chain | Residue |
| A | HOH1574 |
| A | GLN253 |
| A | THR257 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1420 |
| Chain | Residue |
| A | HOH1454 |
| A | HOH1480 |
| A | HOH1597 |
| A | HOH1598 |
| A | HOH1654 |
| A | HOH1664 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 410 |
| Chain | Residue |
| B | ASN67 |
| B | THR239 |
| B | PRO241 |
| B | HOH1414 |
| B | HOH1426 |
| B | HOH1432 |
| B | HOH1456 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 410 |
| Chain | Residue |
| C | ASN67 |
| C | THR239 |
| C | PRO241 |
| C | HOH411 |
| C | HOH415 |
| C | HOH417 |
| C | HOH433 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA D 410 |
| Chain | Residue |
| D | ASN67 |
| D | THR239 |
| D | PRO241 |
| D | HOH2448 |
| D | HOH2485 |
| D | HOH2486 |
| D | HOH2487 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG D 2420 |
| Chain | Residue |
| D | GLU207 |
| D | HOH2458 |
| D | HOH2459 |
| D | HOH2460 |
| D | HOH2528 |
| D | HOH2529 |
| D | HOH2530 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | ILE37 |
| A | SER38 |
| A | CYS39 |
| A | CYS42 |
| A | HIS43 |
| A | SER56 |
| A | ILE57 |
| A | ILE66 |
| A | PRO69 |
| A | ASN77 |
| A | GLN80 |
| A | PHE81 |
| A | TRP82 |
| A | ARG85 |
| A | LEU89 |
| A | GLN92 |
| A | PRO96 |
| A | GLU102 |
| A | ILE142 |
| A | GLU146 |
| A | LYS229 |
| A | HOH1469 |
| A | HOH1471 |
| A | HOH1499 |
| A | HOH1603 |
| A | HOH1680 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 402 |
| Chain | Residue |
| A | TRP82 |
| A | PHE178 |
| A | GLY182 |
| A | CYS183 |
| A | GLN185 |
| A | CYS186 |
| A | HIS187 |
| A | MET200 |
| A | PHE228 |
| A | PRO231 |
| A | LEU233 |
| A | ILE236 |
| A | TYR242 |
| A | PHE243 |
| A | HIS244 |
| A | MET258 |
| A | GLN262 |
| A | LEU263 |
| A | PHE267 |
| A | HOH1423 |
| A | HOH1426 |
| A | HOH1437 |
| A | HOH1458 |
| site_id | BC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | ILE57 |
| B | ILE66 |
| B | ALA68 |
| B | PRO69 |
| B | ASN77 |
| B | GLN80 |
| B | PHE81 |
| B | TRP82 |
| B | ARG85 |
| B | LEU89 |
| B | GLN92 |
| B | PRO96 |
| B | GLU102 |
| B | ILE142 |
| B | GLU146 |
| B | LYS229 |
| B | HOH1419 |
| B | HOH1461 |
| B | HOH1511 |
| B | HOH1513 |
| B | HOH1609 |
| B | ILE37 |
| B | SER38 |
| B | CYS39 |
| B | CYS42 |
| B | HIS43 |
| B | SER56 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 402 |
| Chain | Residue |
| B | TRP82 |
| B | PHE178 |
| B | CYS183 |
| B | CYS186 |
| B | HIS187 |
| B | GLN198 |
| B | MET200 |
| B | VAL202 |
| B | PHE228 |
| B | PRO231 |
| B | ILE236 |
| B | TYR242 |
| B | PHE243 |
| B | HIS244 |
| B | ALA254 |
| B | MET258 |
| B | GLN262 |
| B | LEU263 |
| B | PHE267 |
| B | HOH1426 |
| B | HOH1432 |
| B | HOH1450 |
| B | HOH1462 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM C 401 |
| Chain | Residue |
| C | ILE37 |
| C | SER38 |
| C | CYS39 |
| C | CYS42 |
| C | HIS43 |
| C | SER56 |
| C | ILE57 |
| C | ILE66 |
| C | PRO69 |
| C | ASN77 |
| C | GLN80 |
| C | PHE81 |
| C | TRP82 |
| C | ARG85 |
| C | LEU89 |
| C | GLN92 |
| C | PRO96 |
| C | GLU102 |
| C | ILE142 |
| C | GLU146 |
| C | LYS229 |
| C | HOH453 |
| C | HOH468 |
| C | HOH503 |
| C | HOH605 |
| C | HOH689 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 402 |
| Chain | Residue |
| C | TRP82 |
| C | PHE178 |
| C | CYS183 |
| C | GLN185 |
| C | CYS186 |
| C | HIS187 |
| C | MET200 |
| C | PHE228 |
| C | PRO231 |
| C | LEU233 |
| C | ILE236 |
| C | PHE243 |
| C | HIS244 |
| C | MET258 |
| C | GLN262 |
| C | LEU263 |
| C | PHE267 |
| C | HOH413 |
| C | HOH415 |
| C | HOH433 |
| C | HOH436 |
| site_id | BC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM D 401 |
| Chain | Residue |
| D | PHE26 |
| D | ILE37 |
| D | CYS39 |
| D | CYS42 |
| D | HIS43 |
| D | SER56 |
| D | ILE66 |
| D | PRO69 |
| D | ASN77 |
| D | GLN80 |
| D | PHE81 |
| D | TRP82 |
| D | ARG85 |
| D | LEU89 |
| D | GLN92 |
| D | ALA93 |
| D | PRO96 |
| D | GLU102 |
| D | ILE142 |
| D | GLU146 |
| D | LYS229 |
| D | HOH2510 |
| D | HOH2540 |
| site_id | BC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM D 402 |
| Chain | Residue |
| D | TRP82 |
| D | PHE178 |
| D | GLY182 |
| D | CYS183 |
| D | CYS186 |
| D | HIS187 |
| D | GLN198 |
| D | MET200 |
| D | PHE228 |
| D | PRO231 |
| D | LEU233 |
| D | ILE236 |
| D | PHE243 |
| D | HIS244 |
| D | MET258 |
| D | GLN262 |
| D | LEU263 |
| D | PHE267 |
| D | HOH2448 |
| D | HOH2486 |
| D | HOH2534 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1410 |
| Chain | Residue |
| B | ARG215 |
| B | HOH1486 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433 |
| Chain | Residue | Details |
| A | CYS39 | |
| C | CYS42 | |
| C | CYS183 | |
| C | CYS186 | |
| D | CYS39 | |
| D | CYS42 | |
| D | CYS183 | |
| D | CYS186 | |
| A | CYS42 | |
| A | CYS183 | |
| A | CYS186 | |
| B | CYS39 | |
| B | CYS42 | |
| B | CYS183 | |
| B | CYS186 | |
| C | CYS39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433 |
| Chain | Residue | Details |
| A | HIS43 | |
| C | HIS187 | |
| C | HIS244 | |
| C | MET258 | |
| D | HIS43 | |
| D | HIS187 | |
| D | HIS244 | |
| D | MET258 | |
| A | HIS187 | |
| A | HIS244 | |
| A | MET258 | |
| B | HIS43 | |
| B | HIS187 | |
| B | HIS244 | |
| B | MET258 | |
| C | HIS43 |
