2DE6
The reduced complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
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 | 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 | 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 |
F | 0008901 | molecular_function | ferredoxin hydrogenase activity |
F | 0046232 | biological_process | carbazole catabolic process |
F | 0046872 | molecular_function | metal ion binding |
F | 0051213 | molecular_function | dioxygenase activity |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 A 501 |
Chain | Residue |
A | HIS183 |
A | HIS187 |
A | ASP333 |
A | HOH902 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 B 501 |
Chain | Residue |
B | HIS183 |
B | HIS187 |
B | ASP333 |
B | HOH899 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 C 501 |
Chain | Residue |
C | HIS187 |
C | ASP333 |
C | HOH879 |
C | HIS183 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES A 401 |
Chain | Residue |
A | CYS69 |
A | HIS71 |
A | ARG72 |
A | CYS90 |
A | TYR92 |
A | HIS93 |
A | TRP95 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES B 401 |
Chain | Residue |
B | CYS69 |
B | HIS71 |
B | ARG72 |
B | CYS90 |
B | TYR92 |
B | HIS93 |
B | ALA94 |
B | TRP95 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES C 401 |
Chain | Residue |
C | CYS69 |
C | HIS71 |
C | ARG72 |
C | CYS90 |
C | TYR92 |
C | HIS93 |
C | TRP95 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES D 201 |
Chain | Residue |
D | CYS46 |
D | HIS48 |
D | GLY49 |
D | CYS65 |
D | HIS68 |
D | GLY70 |
D | HOH207 |
site_id | AC8 |
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 | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES F 201 |
Chain | Residue |
F | CYS46 |
F | HIS48 |
F | GLY49 |
F | CYS65 |
F | HIS68 |
F | GLY70 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368 |
Chain | Residue | Details |
D | CYS46 | |
F | HIS48 | |
F | CYS65 | |
F | HIS68 | |
D | HIS48 | |
D | CYS65 | |
D | HIS68 | |
E | CYS46 | |
E | HIS48 | |
E | CYS65 | |
E | HIS68 | |
F | CYS46 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
A | ASP180 | |
A | HIS183 | |
B | HIS93 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
C | HIS93 | |
B | ASP180 | |
B | HIS183 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
A | HIS93 | |
C | HIS183 | |
C | ASP180 |