7BUI
Complex of reduced oxygenase and oxidized ferredoxin in carbazole 1,9a- dioxygenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
D | 0019439 | biological_process | obsolete aromatic compound catabolic process |
D | 0046232 | biological_process | carbazole catabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
E | 0008901 | molecular_function | ferredoxin hydrogenase activity |
E | 0019439 | biological_process | obsolete aromatic compound catabolic process |
E | 0046232 | biological_process | carbazole catabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0051213 | molecular_function | dioxygenase activity |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue FES A 401 |
Chain | Residue |
A | CYS69 |
A | HIS71 |
A | ARG72 |
A | CYS90 |
A | HIS93 |
A | TRP95 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue FE2 A 402 |
Chain | Residue |
A | HOH590 |
A | HIS183 |
A | HIS187 |
A | ASP333 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | GLY244 |
B | THR87 |
B | ARG98 |
B | ASP106 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | VAL32 |
A | MET33 |
A | GLU37 |
A | ASN164 |
A | HOH514 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | ASP20 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue FES B 401 |
Chain | Residue |
B | CYS69 |
B | HIS71 |
B | ARG72 |
B | CYS90 |
B | TYR92 |
B | HIS93 |
B | TRP95 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue FE2 B 402 |
Chain | Residue |
B | HIS183 |
B | HIS187 |
B | ASP333 |
B | HOH679 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PEG B 403 |
Chain | Residue |
B | MET33 |
B | GLU37 |
B | ASN164 |
B | ILE166 |
B | HOH598 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | LYS47 |
B | GLY50 |
B | GLN379 |
B | HOH596 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | LYS168 |
B | ASN292 |
B | VAL341 |
B | HOH621 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | ASP20 |
B | HOH543 |
B | HOH658 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | GLY162 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue FES C 401 |
Chain | Residue |
C | CYS69 |
C | HIS71 |
C | ARG72 |
C | VAL74 |
C | CYS90 |
C | HIS93 |
C | TRP95 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue FE2 C 402 |
Chain | Residue |
C | HIS183 |
C | HIS187 |
C | ASP333 |
C | HOH610 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue EDO C 403 |
Chain | Residue |
C | LYS47 |
C | ASN52 |
C | HOH573 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO C 404 |
Chain | Residue |
C | LYS79 |
C | VAL80 |
C | HOH606 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
C | ASP189 |
C | ILE191 |
C | GLY328 |
C | ASP332 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue FES D 201 |
Chain | Residue |
D | CYS46 |
D | HIS48 |
D | GLY49 |
D | CYS65 |
D | HIS68 |
D | GLY70 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue FES E 201 |
Chain | Residue |
E | CYS46 |
E | HIS48 |
E | GLY49 |
E | CYS65 |
E | HIS68 |
E | GLY70 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue PEG E 202 |
Chain | Residue |
E | TRP5 |
E | GLU94 |
E | LYS96 |
E | TYR101 |
E | HOH316 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368 |
Chain | Residue | Details |
D | CYS46 | |
E | CYS46 | |
E | HIS48 | |
E | CYS65 | |
E | HIS68 | |
D | HIS48 | |
D | CYS65 | |
D | HIS68 |