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 | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
A | 0042574 | biological_process | retinal metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
B | 0042574 | biological_process | retinal metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
C | 0042574 | biological_process | retinal metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
D | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
D | 0042574 | biological_process | retinal metabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
E | 0042574 | biological_process | retinal metabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0051213 | molecular_function | dioxygenase activity |
F | 0003834 | molecular_function | beta-carotene 15,15'-dioxygenase activity |
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 |
F | 0042574 | biological_process | retinal metabolic process |
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 |