1VCK
Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046232 | biological_process | carbazole catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 211 |
Chain | Residue |
A | GLU55 |
A | GLU55 |
A | H2S212 |
A | H2S212 |
A | HOH260 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES A 201 |
Chain | Residue |
A | PHE67 |
A | HIS68 |
A | GLY70 |
A | CYS84 |
A | CYS46 |
A | HIS48 |
A | GLY49 |
A | CYS65 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE H2S A 212 |
Chain | Residue |
A | GLU55 |
A | FE211 |
A | FE211 |
A | HOH329 |
A | HOH329 |
A | HOH348 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 96 |
Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15645447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17161368","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
A | HIS68 |