6LLF
Biphenyl-2,2',3-triol-soaked resting complex of Oxy and Fd in carbazole 1,9a-dioxygenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046232 | biological_process | carbazole catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046232 | biological_process | carbazole catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046232 | biological_process | carbazole catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 401 |
| Chain | Residue |
| A | CYS69 |
| A | HIS71 |
| A | ARG72 |
| A | VAL74 |
| A | CYS90 |
| A | TYR92 |
| A | HIS93 |
| A | TRP95 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 402 |
| Chain | Residue |
| A | HIS187 |
| A | ASP333 |
| A | WBP403 |
| A | HOH501 |
| A | HIS183 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue WBP A 403 |
| Chain | Residue |
| A | GLY178 |
| A | HIS183 |
| A | ILE184 |
| A | LEU200 |
| A | ALA259 |
| A | ILE262 |
| A | LEU270 |
| A | PHE275 |
| A | GLN282 |
| A | GLU284 |
| A | PHE329 |
| A | ASN330 |
| A | ASP333 |
| A | FE2402 |
| A | HOH501 |
| A | HOH571 |
| A | HOH591 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LYS130 |
| A | GLU159 |
| A | ILE160 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | PRO17 |
| A | ASP20 |
| A | HOH714 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ARG68 |
| A | SER383 |
| A | HOH518 |
| A | HOH537 |
| A | HOH829 |
| C | PHE343 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | MET33 |
| A | GLU37 |
| A | ASN164 |
| A | TYR295 |
| A | HOH618 |
| A | HOH646 |
| A | HOH684 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue PGE A 408 |
| Chain | Residue |
| A | ASP229 |
| A | ILE231 |
| A | GLY232 |
| A | GLU233 |
| A | ASN260 |
| A | ILE262 |
| A | HOH588 |
| A | HOH696 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | TYR228 |
| A | EDO410 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ARG215 |
| A | EDO409 |
| A | HOH508 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | CYS82 |
| A | LYS83 |
| A | THR84 |
| A | LYS85 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 412 |
| Chain | Residue |
| A | SER86 |
| A | ARG98 |
| A | CYS105 |
| A | HOH511 |
| A | HOH624 |
| C | GLY244 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue FES B 401 |
| Chain | Residue |
| B | CYS69 |
| B | HIS71 |
| B | ARG72 |
| B | CYS90 |
| B | HIS93 |
| B | ALA94 |
| B | TRP95 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 402 |
| Chain | Residue |
| B | HIS183 |
| B | HIS187 |
| B | ASP333 |
| B | WBP403 |
| B | HOH569 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue WBP B 403 |
| Chain | Residue |
| B | HOH780 |
| B | GLY178 |
| B | HIS183 |
| B | ILE184 |
| B | ALA259 |
| B | ILE262 |
| B | LEU270 |
| B | PHE275 |
| B | GLN282 |
| B | GLU284 |
| B | PHE329 |
| B | ASN330 |
| B | FE2402 |
| B | HOH508 |
| B | HOH569 |
| B | HOH582 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 404 |
| Chain | Residue |
| A | TRP335 |
| B | VAL78 |
| B | LYS79 |
| B | HOH813 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| A | PHE343 |
| A | HOH687 |
| B | ARG68 |
| B | SER383 |
| B | HOH515 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | TRP335 |
| C | VAL78 |
| site_id | AE1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | LYS163 |
| B | GLN165 |
| B | TYR296 |
| B | GLN298 |
| B | LEU326 |
| B | ASN330 |
| B | ASN331 |
| B | ILE334 |
| B | HOH714 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | LYS188 |
| B | ASP189 |
| B | SER190 |
| B | VAL193 |
| B | LYS194 |
| B | HOH655 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | ASP101 |
| B | LYS120 |
| B | LEU121 |
| B | LYS122 |
| B | THR123 |
| B | HOH821 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue FES C 401 |
| Chain | Residue |
| C | CYS69 |
| C | HIS71 |
| C | ARG72 |
| C | CYS90 |
| C | TYR92 |
| C | HIS93 |
| C | ALA94 |
| C | TRP95 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 C 402 |
| Chain | Residue |
| C | HIS183 |
| C | HIS187 |
| C | ASP333 |
| C | WBP403 |
| C | HOH501 |
| site_id | AE6 |
| Number of Residues | 16 |
| Details | binding site for residue WBP C 403 |
| Chain | Residue |
| C | GLY178 |
| C | HIS183 |
| C | ILE184 |
| C | ALA259 |
| C | ILE262 |
| C | LEU270 |
| C | PHE275 |
| C | GLN282 |
| C | GLU284 |
| C | PHE329 |
| C | ASN330 |
| C | FE2402 |
| C | HOH501 |
| C | HOH591 |
| C | HOH638 |
| C | HOH820 |
| site_id | AE7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| C | PHE204 |
| C | ASP229 |
| C | LEU230 |
| C | ILE231 |
| C | GLY232 |
| C | ALA259 |
| C | HOH556 |
| C | HOH606 |
| site_id | AE8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| B | TYR185 |
| B | ILE186 |
| B | LYS188 |
| B | TRP335 |
| B | HOH607 |
| C | LYS79 |
| C | GLU81 |
| C | TRP91 |
| site_id | AE9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 406 |
| Chain | Residue |
| B | THR242 |
| C | ASP106 |
| C | ILE107 |
| C | LEU108 |
| C | PRO111 |
| C | ILE116 |
| C | HOH512 |
| C | HOH530 |
| site_id | AF1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 407 |
| Chain | Residue |
| C | ASP20 |
| C | HOH727 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 408 |
| Chain | Residue |
| C | GLN119 |
| C | LYS120 |
| C | HOH608 |
| E | THR85 |
| E | VAL86 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue FES D 201 |
| Chain | Residue |
| D | CYS46 |
| D | HIS48 |
| D | GLY49 |
| D | CYS65 |
| D | HIS68 |
| D | GLY70 |
| site_id | AF4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 202 |
| Chain | Residue |
| D | GLY17 |
| D | THR18 |
| D | GLY56 |
| D | THR57 |
| D | LEU58 |
| D | HOH304 |
| site_id | AF5 |
| Number of Residues | 6 |
| Details | binding site for residue FES E 201 |
| Chain | Residue |
| E | CYS46 |
| E | HIS48 |
| E | GLY49 |
| E | CYS65 |
| E | HIS68 |
| E | GLY70 |
| site_id | AF6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO E 202 |
| Chain | Residue |
| E | LYS106 |
| E | HOH312 |
| site_id | AF7 |
| Number of Residues | 6 |
| Details | binding site for residue FES F 201 |
| Chain | Residue |
| F | CYS46 |
| F | HIS48 |
| F | GLY49 |
| F | CYS65 |
| F | HIS68 |
| F | GLY70 |
| site_id | AF8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO F 202 |
| Chain | Residue |
| F | GLY17 |
| F | GLY56 |
| F | LEU58 |
| F | HOH308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI7 |
| Number of Residues | 288 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15645447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17161368","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






