6VCF
Crystal structure of Nitrosotalea devanaterra carotenoid cleavage dioxygenase, iron form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010436 | molecular_function | carotenoid dioxygenase activity |
| A | 0016121 | biological_process | carotene catabolic process |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0010436 | molecular_function | carotenoid dioxygenase activity |
| B | 0016121 | biological_process | carotene catabolic process |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0010436 | molecular_function | carotenoid dioxygenase activity |
| C | 0016121 | biological_process | carotene catabolic process |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0010436 | molecular_function | carotenoid dioxygenase activity |
| D | 0016121 | biological_process | carotene catabolic process |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| E | 0010436 | molecular_function | carotenoid dioxygenase activity |
| E | 0016121 | biological_process | carotene catabolic process |
| E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| F | 0010436 | molecular_function | carotenoid dioxygenase activity |
| F | 0016121 | biological_process | carotene catabolic process |
| F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 A 501 |
| Chain | Residue |
| A | HIS172 |
| A | HIS222 |
| A | HIS289 |
| A | HIS467 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | LYS241 |
| A | PRO242 |
| A | LEU243 |
| B | GLU216 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 503 |
| Chain | Residue |
| A | SER383 |
| C | GLU354 |
| C | SER378 |
| C | THR379 |
| C | GLN388 |
| A | ALA382 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 501 |
| Chain | Residue |
| B | HIS172 |
| B | HIS222 |
| B | HIS289 |
| B | HIS467 |
| B | BCT502 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue BCT B 502 |
| Chain | Residue |
| B | PHE58 |
| B | VAL126 |
| B | HIS222 |
| B | HIS289 |
| B | PHE466 |
| B | HIS467 |
| B | FE2501 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| B | GLU354 |
| B | SER378 |
| B | THR379 |
| B | GLN388 |
| D | ALA382 |
| D | SER383 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 C 501 |
| Chain | Residue |
| C | HIS172 |
| C | HIS222 |
| C | HIS289 |
| C | HIS467 |
| C | BCT502 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue BCT C 502 |
| Chain | Residue |
| C | PHE58 |
| C | VAL126 |
| C | HIS222 |
| C | HIS289 |
| C | PHE466 |
| C | HIS467 |
| C | FE2501 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 D 1000 |
| Chain | Residue |
| D | HIS172 |
| D | HIS222 |
| D | HIS289 |
| D | HIS467 |
| D | HOH1135 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 E 1000 |
| Chain | Residue |
| E | HIS172 |
| E | HIS222 |
| E | HIS289 |
| E | HIS467 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 F 1000 |
| Chain | Residue |
| F | HIS172 |
| F | HIS222 |
| F | HIS289 |
| F | HIS467 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 30 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. maytvtnkfqlgfstlseeldl.............................................................................................ESLQVKGT |
| Chain | Residue | Details |
| A | MET1-THR30 |
