3IC9
The structure of dihydrolipoamide dehydrogenase from Colwellia psychrerythraea 34H.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 490 |
| Chain | Residue |
| A | ILE11 |
| A | GLY47 |
| A | CYS48 |
| A | SER51 |
| A | LYS52 |
| A | GLY114 |
| A | PHE115 |
| A | ALA116 |
| A | ALA140 |
| A | THR141 |
| A | GLY142 |
| A | GLY12 |
| A | ASN161 |
| A | LEU276 |
| A | GLY309 |
| A | ASP310 |
| A | THR316 |
| A | LEU317 |
| A | LEU318 |
| A | PHE351 |
| A | HOH509 |
| A | HOH520 |
| A | GLY14 |
| A | HOH524 |
| A | HOH531 |
| A | HOH555 |
| A | HOH588 |
| A | HOH602 |
| A | HOH610 |
| B | TYR448 |
| B | HIS449 |
| B | HOH631 |
| A | THR15 |
| A | ALA16 |
| A | GLU35 |
| A | GLY36 |
| A | THR42 |
| A | VAL46 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 491 |
| Chain | Residue |
| A | GLY309 |
| A | ASN312 |
| A | THR314 |
| A | ASP324 |
| A | HOH633 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 490 |
| Chain | Residue |
| A | TYR448 |
| A | HIS449 |
| B | ILE11 |
| B | GLY12 |
| B | GLY14 |
| B | THR15 |
| B | ALA16 |
| B | GLU35 |
| B | GLY36 |
| B | THR42 |
| B | VAL46 |
| B | GLY47 |
| B | CYS48 |
| B | SER51 |
| B | LYS52 |
| B | GLY114 |
| B | PHE115 |
| B | ALA116 |
| B | ALA140 |
| B | THR141 |
| B | GLY142 |
| B | ASN161 |
| B | ILE182 |
| B | ARG269 |
| B | LEU276 |
| B | GLY309 |
| B | ASP310 |
| B | THR316 |
| B | LEU317 |
| B | LEU318 |
| B | ALA321 |
| B | PHE351 |
| B | HOH515 |
| B | HOH572 |
| B | HOH584 |
| B | HOH619 |
| B | HOH625 |
| B | HOH649 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 491 |
| Chain | Residue |
| B | GLY309 |
| B | ASN312 |
| B | THR314 |
| B | ASP324 |
| B | HOH610 |
| B | HOH821 |
| site_id | AC5 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD C 490 |
| Chain | Residue |
| C | LYS52 |
| C | GLY114 |
| C | PHE115 |
| C | ALA116 |
| C | ALA140 |
| C | THR141 |
| C | GLY142 |
| C | ASN161 |
| C | ILE182 |
| C | ARG269 |
| C | LEU276 |
| C | GLY309 |
| C | ASP310 |
| C | THR316 |
| C | LEU317 |
| C | LEU318 |
| C | PHE351 |
| C | HOH495 |
| C | HOH533 |
| C | HOH545 |
| C | HOH558 |
| C | HOH559 |
| C | HOH612 |
| C | HOH648 |
| C | HOH662 |
| C | HOH696 |
| C | HOH864 |
| D | TYR448 |
| D | HIS449 |
| C | ILE11 |
| C | GLY12 |
| C | GLY14 |
| C | THR15 |
| C | ALA16 |
| C | GLU35 |
| C | GLY36 |
| C | THR42 |
| C | VAL46 |
| C | GLY47 |
| C | CYS48 |
| C | SER51 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 491 |
| Chain | Residue |
| C | GLY309 |
| C | ASN312 |
| C | THR314 |
| C | ASP324 |
| C | HOH848 |
| site_id | AC7 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD D 490 |
| Chain | Residue |
| C | TYR448 |
| C | HIS449 |
| D | ILE11 |
| D | GLY12 |
| D | GLY14 |
| D | THR15 |
| D | ALA16 |
| D | GLU35 |
| D | GLY36 |
| D | THR42 |
| D | GLY47 |
| D | CYS48 |
| D | SER51 |
| D | LYS52 |
| D | GLY114 |
| D | PHE115 |
| D | ALA116 |
| D | ALA140 |
| D | THR141 |
| D | GLY142 |
| D | ASN161 |
| D | ILE182 |
| D | ARG269 |
| D | GLY309 |
| D | ASP310 |
| D | THR316 |
| D | LEU317 |
| D | LEU318 |
| D | PHE351 |
| D | HOH518 |
| D | HOH527 |
| D | HOH549 |
| D | HOH569 |
| D | HOH575 |
| D | HOH582 |
| D | HOH615 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 491 |
| Chain | Residue |
| D | GLY309 |
| D | ASN312 |
| D | THR314 |
| D | ASP324 |
| D | HOH697 |
| D | HOH925 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS48 | |
| A | CYS43 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS48 | |
| B | CYS43 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| C | CYS48 | |
| C | CYS43 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | CYS48 | |
| D | CYS43 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU454 | |
| A | HIS449 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU454 | |
| B | HIS449 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| C | GLU454 | |
| C | HIS449 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | GLU454 | |
| D | HIS449 |
