6VCH
Crystal structure of Nitrosotalea devanaterra carotenoid cleavage dioxygenase in complex with 3-hydroxy-beta-apo-14'-carotenal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010436 | molecular_function | carotenoid dioxygenase activity |
| A | 0016121 | biological_process | carotene catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0010436 | molecular_function | carotenoid dioxygenase activity |
| B | 0016121 | biological_process | carotene catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0010436 | molecular_function | carotenoid dioxygenase activity |
| C | 0016121 | biological_process | carotene catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0010436 | molecular_function | carotenoid dioxygenase activity |
| D | 0016121 | biological_process | carotene catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| E | 0010436 | molecular_function | carotenoid dioxygenase activity |
| E | 0016121 | biological_process | carotene catabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| F | 0010436 | molecular_function | carotenoid dioxygenase activity |
| F | 0016121 | biological_process | carotene catabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CO A 501 |
| Chain | Residue |
| A | HIS172 |
| A | HIS222 |
| A | HIS289 |
| A | HIS467 |
| A | HOH604 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue QVM A 502 |
| Chain | Residue |
| A | PHE120 |
| A | THR121 |
| A | ASN125 |
| A | VAL126 |
| A | THR139 |
| A | GLU140 |
| A | GLY167 |
| A | HIS222 |
| A | PHE252 |
| A | HOH604 |
| A | PHE58 |
| A | ARG98 |
| A | GLU99 |
| A | PHE100 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | PRO242 |
| A | LEU243 |
| B | GLU216 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CO B 501 |
| Chain | Residue |
| B | HIS172 |
| B | HIS222 |
| B | HIS289 |
| B | HIS467 |
| B | HOH601 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| B | GLU354 |
| B | SER378 |
| B | THR379 |
| B | GLN388 |
| D | ALA382 |
| D | SER383 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue QVM B 503 |
| Chain | Residue |
| B | PHE58 |
| B | ARG98 |
| B | GLU99 |
| B | PHE100 |
| B | PHE120 |
| B | THR121 |
| B | ASN125 |
| B | VAL126 |
| B | THR139 |
| B | GLU140 |
| B | GLY167 |
| B | HIS222 |
| B | PHE252 |
| B | HOH601 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CO C 501 |
| Chain | Residue |
| C | HIS172 |
| C | HIS222 |
| C | HIS289 |
| C | HIS467 |
| C | HOH604 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue QVM C 502 |
| Chain | Residue |
| C | PHE58 |
| C | ARG98 |
| C | GLU99 |
| C | PHE100 |
| C | PHE120 |
| C | THR121 |
| C | ASN125 |
| C | VAL126 |
| C | THR139 |
| C | GLU140 |
| C | GLY167 |
| C | HIS222 |
| C | PHE252 |
| C | HOH604 |
| C | HOH647 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 503 |
| Chain | Residue |
| A | ALA382 |
| A | SER383 |
| C | GLU354 |
| C | SER378 |
| C | THR379 |
| C | GLN388 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CO D 501 |
| Chain | Residue |
| D | HIS172 |
| D | HIS222 |
| D | HIS289 |
| D | HIS467 |
| D | HOH605 |
| site_id | AD2 |
| Number of Residues | 17 |
| Details | binding site for residue QVM D 502 |
| Chain | Residue |
| D | PHE58 |
| D | ARG98 |
| D | GLU99 |
| D | PHE100 |
| D | PHE120 |
| D | THR121 |
| D | ASN125 |
| D | VAL126 |
| D | THR139 |
| D | GLU140 |
| D | THR141 |
| D | GLY167 |
| D | HIS222 |
| D | PHE252 |
| D | HOH605 |
| D | HOH629 |
| D | HOH634 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CO E 501 |
| Chain | Residue |
| E | HOH605 |
| E | HIS172 |
| E | HIS222 |
| E | HIS289 |
| E | HIS467 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue CL E 502 |
| Chain | Residue |
| E | ASN208 |
| F | ASN208 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CO 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 |
