3VMI
Carbazole- and oxygen-bound complex between oxygenase and ferredoxin 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 | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 A 501 |
| Chain | Residue |
| A | HIS183 |
| A | HIS187 |
| A | ASP333 |
| A | OXY601 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 401 |
| Chain | Residue |
| A | TYR92 |
| A | HIS93 |
| A | TRP95 |
| A | CYS69 |
| A | HIS71 |
| A | ARG72 |
| A | VAL74 |
| A | CYS90 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXY A 601 |
| Chain | Residue |
| A | HIS183 |
| A | HIS187 |
| A | PHE329 |
| A | ASN330 |
| A | ASP333 |
| A | FE2501 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 B 501 |
| Chain | Residue |
| B | HIS183 |
| B | HIS187 |
| B | ASP333 |
| B | OXY602 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 401 |
| Chain | Residue |
| B | CYS69 |
| B | HIS71 |
| B | ARG72 |
| B | CYS90 |
| B | TYR92 |
| B | HIS93 |
| B | TRP95 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXY B 602 |
| Chain | Residue |
| B | HIS183 |
| B | HIS187 |
| B | PHE329 |
| B | ASN330 |
| B | ASP333 |
| B | HOH431 |
| B | FE2501 |
| B | 9CA2001 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 9CA B 2001 |
| Chain | Residue |
| B | GLY178 |
| B | HIS183 |
| B | ILE184 |
| B | ILE262 |
| B | LEU270 |
| B | VAL272 |
| B | PHE275 |
| B | GLN282 |
| B | GLU284 |
| B | PHE329 |
| B | ASN330 |
| B | OXY602 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 C 501 |
| Chain | Residue |
| C | HIS183 |
| C | HIS187 |
| C | ASP333 |
| C | OXY603 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 401 |
| Chain | Residue |
| C | CYS69 |
| C | HIS71 |
| C | ARG72 |
| C | CYS90 |
| C | TYR92 |
| C | HIS93 |
| C | TRP95 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXY C 603 |
| Chain | Residue |
| C | HIS183 |
| C | HIS187 |
| C | PHE329 |
| C | ASP333 |
| C | FE2501 |
| C | 9CA2002 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 9CA C 2002 |
| Chain | Residue |
| C | GLY178 |
| C | HIS183 |
| C | ILE184 |
| C | ILE262 |
| C | LEU270 |
| C | PHE275 |
| C | GLN282 |
| C | PHE329 |
| C | ASN330 |
| C | OXY603 |
| site_id | BC3 |
| 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 | BC4 |
| 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 | BC5 |
| 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_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 |
