6VCF
Crystal structure of Nitrosotalea devanaterra carotenoid cleavage dioxygenase, iron form
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 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 | 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 | 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 |