Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0043448 | biological_process | alkane catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0043448 | biological_process | alkane catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0043448 | biological_process | alkane catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS6 |
| A | CYS9 |
| A | CYS39 |
| A | CYS42 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 302 |
| Chain | Residue |
| B | CYS106 |
| B | CYS109 |
| B | CYS139 |
| B | CYS142 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 303 |
| Chain | Residue |
| C | CYS209 |
| C | CYS239 |
| C | CYS242 |
| C | CYS206 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 401 |
| Chain | Residue |
| B | PRO120 |
| C | ASP235 |
| C | SER247 |
| C | HOH1139 |
| C | HOH1173 |
| C | HOH1174 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 501 |
| Chain | Residue |
| A | PRO45 |
| A | LYS46 |
| A | SER47 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 601 |
| Chain | Residue |
| A | MET1 |
| A | LYS2 |
| A | TYR4 |
| A | ASP29 |
| A | LYS31 |
| A | HOH1248 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 701 |
| Chain | Residue |
| B | ASP135 |
| B | PRO145 |
| B | LYS146 |
| B | SER147 |
| B | HOH1067 |
| B | HOH1143 |
| B | HOH1225 |
Functional Information from PROSITE/UniProt
| site_id | PS00202 |
| Number of Residues | 11 |
| Details | RUBREDOXIN Rubredoxin signature. IpDDWvCPiCG |
| Chain | Residue | Details |
| A | ILE33-GLY43 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
