2B24
Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. bound to indole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| A | 0044237 | biological_process | cellular metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
| B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| C | 0044237 | biological_process | cellular metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
| D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| D | 0051213 | molecular_function | dioxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| E | 0044237 | biological_process | cellular metabolic 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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
| F | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE A 502 |
| Chain | Residue |
| A | HIS216 |
| A | HIS221 |
| A | ASP372 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE C 502 |
| Chain | Residue |
| C | HIS216 |
| C | HIS221 |
| C | ASP372 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE E 502 |
| Chain | Residue |
| E | HIS216 |
| E | HIS221 |
| E | ASP372 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 501 |
| Chain | Residue |
| A | CYS88 |
| A | HIS90 |
| A | ARG91 |
| A | CYS108 |
| A | HIS111 |
| A | GLY112 |
| A | TRP113 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IND A 503 |
| Chain | Residue |
| A | ASP213 |
| A | HIS295 |
| A | PHE307 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES C 501 |
| Chain | Residue |
| C | CYS88 |
| C | HIS90 |
| C | ARG91 |
| C | CYS108 |
| C | TYR110 |
| C | HIS111 |
| C | GLY112 |
| C | TRP113 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IND C 503 |
| Chain | Residue |
| C | ASP213 |
| C | HIS295 |
| C | PHE307 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES E 501 |
| Chain | Residue |
| E | CYS88 |
| E | HIS90 |
| E | ARG91 |
| E | CYS108 |
| E | TYR110 |
| E | HIS111 |
| E | GLY112 |
| E | TRP113 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IND E 503 |
| Chain | Residue |
| E | ASP213 |
| E | HIS295 |
| E | PHE307 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmqvcraemGNtshfrCpYH |
| Chain | Residue | Details |
| A | CYS88-HIS111 |
