3LB8
Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0019383 | biological_process | (+)-camphor catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0019383 | biological_process | (+)-camphor catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0140647 | biological_process | P450-containing electron transport chain |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0022900 | biological_process | electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0140647 | biological_process | P450-containing electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 449 |
| Chain | Residue |
| A | HOH1 |
| A | SER49 |
| A | LYS50 |
| A | THR81 |
| A | GLN82 |
| A | VAL83 |
| A | ALA109 |
| A | THR110 |
| A | GLY111 |
| A | GLY112 |
| A | ARG134 |
| A | GLY11 |
| A | ILE160 |
| A | ASP284 |
| A | GLU300 |
| A | SER301 |
| A | VAL302 |
| A | PRO303 |
| A | PHE329 |
| A | TRP330 |
| A | HOH438 |
| A | HOH439 |
| A | GLY13 |
| A | HOH471 |
| A | HOH475 |
| A | LEU14 |
| A | ALA15 |
| A | GLY36 |
| A | ASP37 |
| A | LEU45 |
| A | PRO46 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD B 449 |
| Chain | Residue |
| B | VAL10 |
| B | GLY11 |
| B | GLY13 |
| B | LEU14 |
| B | ALA15 |
| B | GLY36 |
| B | ASP37 |
| B | LEU45 |
| B | PRO46 |
| B | SER49 |
| B | LYS50 |
| B | THR81 |
| B | VAL83 |
| B | ALA109 |
| B | THR110 |
| B | GLY111 |
| B | GLY112 |
| B | LEU133 |
| B | ARG134 |
| B | ILE160 |
| B | ASN251 |
| B | LEU254 |
| B | GLY283 |
| B | ASP284 |
| B | GLU300 |
| B | SER301 |
| B | VAL302 |
| B | PRO303 |
| B | PHE329 |
| B | TRP330 |
| B | HOH438 |
| B | HOH443 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES C 107 |
| Chain | Residue |
| C | GLY37 |
| C | CYS39 |
| C | GLY41 |
| C | ALA43 |
| C | SER44 |
| C | CYS45 |
| C | ALA46 |
| C | CYS48 |
| C | CYS86 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FES D 107 |
| Chain | Residue |
| D | GLY37 |
| D | CYS39 |
| D | GLY40 |
| D | GLY41 |
| D | ALA43 |
| D | SER44 |
| D | CYS45 |
| D | CYS48 |
| D | LEU84 |
| D | CYS86 |
Functional Information from PROSITE/UniProt
| site_id | PS00814 |
| Number of Residues | 11 |
| Details | ADX Adrenodoxin family, iron-sulfur binding region signature. CggSaSCATCH |
| Chain | Residue | Details |
| C | CYS39-HIS49 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15095867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20179327","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LB8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15095867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20179327","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LB8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8204575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
