4NBF
Oxygenase with Gln282 replaced by Asn and ferredoxin complex of 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 501 |
| Chain | Residue |
| A | HIS183 |
| A | HIS187 |
| A | ASP333 |
| A | HOH710 |
| A | HOH898 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 502 |
| Chain | Residue |
| A | TYR92 |
| A | HIS93 |
| A | TRP95 |
| A | CYS69 |
| A | HIS71 |
| A | ARG72 |
| A | CYS90 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 B 501 |
| Chain | Residue |
| B | HIS183 |
| B | HIS187 |
| B | ASP333 |
| B | HOH869 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 502 |
| Chain | Residue |
| B | CYS69 |
| B | HIS71 |
| B | ARG72 |
| B | CYS90 |
| B | TYR92 |
| B | HIS93 |
| B | TRP95 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C 501 |
| Chain | Residue |
| C | HIS183 |
| C | HIS187 |
| C | ASP333 |
| C | HOH744 |
| C | HOH907 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 502 |
| Chain | Residue |
| C | CYS69 |
| C | HIS71 |
| C | ARG72 |
| C | CYS90 |
| C | TYR92 |
| C | HIS93 |
| C | TRP95 |
| site_id | AC7 |
| 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 | AC8 |
| 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 | AC9 |
| 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 |
