6LLH
Biphenyl-2,3-diol-soaked resting complex of Oxy and Fd in carbazole 1,9a-dioxygenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0046232 | biological_process | carbazole catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| E | 0046232 | biological_process | carbazole catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| F | 0046232 | biological_process | carbazole catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
| F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 A 501 |
| Chain | Residue |
| A | HIS183 |
| A | HIS187 |
| A | ASP333 |
| A | BPY503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue FES A 502 |
| Chain | Residue |
| A | TRP95 |
| A | CYS69 |
| A | HIS71 |
| A | ARG72 |
| A | CYS90 |
| A | HIS93 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue BPY A 503 |
| Chain | Residue |
| A | HIS183 |
| A | HIS187 |
| A | ALA259 |
| A | ILE262 |
| A | LEU270 |
| A | VAL272 |
| A | GLU284 |
| A | PHE329 |
| A | ASN330 |
| A | ASP333 |
| A | FE2501 |
| A | HOH622 |
| A | HOH632 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | LYS130 |
| A | GLU159 |
| A | ILE160 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PGE A 505 |
| Chain | Residue |
| A | PHE204 |
| A | ASP229 |
| A | LEU230 |
| A | GLY232 |
| A | GLU233 |
| A | ALA259 |
| A | ASN260 |
| A | ASP261 |
| A | ILE262 |
| A | HOH617 |
| A | HOH632 |
| A | HOH649 |
| A | HOH849 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 506 |
| Chain | Residue |
| A | SER86 |
| A | ARG98 |
| A | HOH699 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 507 |
| Chain | Residue |
| A | THR242 |
| B | PRO111 |
| E | GLN3 |
| E | ILE4 |
| E | TRP5 |
| E | PEG202 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | LYS36 |
| A | LEU161 |
| A | GLY162 |
| A | HOH634 |
| A | HOH786 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 B 501 |
| Chain | Residue |
| B | HIS183 |
| B | HIS187 |
| B | ASP333 |
| B | HOH720 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue FES B 502 |
| Chain | Residue |
| B | CYS69 |
| B | HIS71 |
| B | ARG72 |
| B | CYS90 |
| B | HIS93 |
| B | ALA94 |
| B | TRP95 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for residue BPY B 503 |
| Chain | Residue |
| B | GLY178 |
| B | HIS183 |
| B | ILE184 |
| B | ALA259 |
| B | ILE262 |
| B | LEU270 |
| B | PHE275 |
| B | GLN282 |
| B | GLU284 |
| B | PHE329 |
| B | ASN330 |
| B | HOH688 |
| B | HOH720 |
| B | HOH759 |
| B | HOH857 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | LYS163 |
| B | GLN165 |
| B | TYR296 |
| B | GLN298 |
| B | LEU326 |
| B | GLU327 |
| B | ASN330 |
| B | ASN331 |
| B | ILE334 |
| B | HOH820 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 505 |
| Chain | Residue |
| A | GLY244 |
| B | SER86 |
| B | ARG98 |
| B | CYS105 |
| B | ASP106 |
| B | HOH676 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| A | PHE343 |
| A | HOH783 |
| B | ARG68 |
| B | HOH644 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | LEU62 |
| B | TYR63 |
| B | PRO125 |
| B | VAL126 |
| B | HOH638 |
| B | HOH684 |
| B | HOH751 |
| B | HOH826 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| B | PHE204 |
| B | ASP229 |
| B | LEU230 |
| B | ILE231 |
| B | GLY232 |
| B | ALA259 |
| B | ASN260 |
| B | HOH675 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 509 |
| Chain | Residue |
| B | LYS36 |
| B | GLY162 |
| B | HOH764 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 C 501 |
| Chain | Residue |
| C | HIS183 |
| C | HIS187 |
| C | ASP333 |
| C | HOH700 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue FES C 502 |
| Chain | Residue |
| C | CYS69 |
| C | HIS71 |
| C | ARG72 |
| C | CYS90 |
| C | TYR92 |
| C | HIS93 |
| C | ALA94 |
| C | TRP95 |
| site_id | AE2 |
| Number of Residues | 13 |
| Details | binding site for residue BPY C 503 |
| 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 | HOH681 |
| C | HOH700 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | PHE204 |
| C | ASP229 |
| C | LEU230 |
| C | ILE231 |
| C | GLY232 |
| C | ALA259 |
| C | HOH625 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 505 |
| Chain | Residue |
| C | VAL32 |
| C | MET33 |
| C | GLU37 |
| C | ASN164 |
| C | HOH613 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 506 |
| Chain | Residue |
| B | THR242 |
| C | ASP106 |
| C | ILE107 |
| C | LEU108 |
| C | PRO111 |
| C | ILE116 |
| C | HOH606 |
| C | HOH620 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 507 |
| Chain | Residue |
| B | TYR185 |
| B | ILE186 |
| B | LYS188 |
| B | TRP335 |
| B | HOH725 |
| C | LYS79 |
| C | GLU81 |
| C | TRP91 |
| site_id | AE7 |
| 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 | AE8 |
| 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 | AE9 |
| Number of Residues | 7 |
| Details | binding site for residue PEG E 202 |
| Chain | Residue |
| A | PEG507 |
| E | TRP5 |
| E | GLU94 |
| E | LYS96 |
| E | TYR101 |
| E | HOH303 |
| E | HOH353 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue PGE E 203 |
| Chain | Residue |
| C | ARG118 |
| C | HOH609 |
| E | GLU43 |
| E | GLY89 |
| E | LYS106 |
| E | HOH330 |
| E | HOH341 |
| site_id | AF2 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368 |
| Chain | Residue | Details |
| D | CYS46 | |
| F | HIS48 | |
| F | CYS65 | |
| F | HIS68 | |
| D | HIS48 | |
| D | CYS65 | |
| D | HIS68 | |
| E | CYS46 | |
| E | HIS48 | |
| E | CYS65 | |
| E | HIS68 | |
| F | CYS46 |
