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 | 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 | 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: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:8204575 |
Chain | Residue | Details |
C | CYS39 | |
C | CYS45 | |
C | CYS48 | |
C | CYS86 | |
D | CYS39 | |
D | CYS45 | |
D | CYS48 | |
D | CYS86 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15095867, ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R, ECO:0007744|PDB:3LB8 |
Chain | Residue | Details |
A | ARG134 | |
A | ASP284 | |
A | VAL302 | |
B | ARG134 | |
B | ASP284 | |
B | VAL302 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY156 | |
B | GLY156 |