1XDI
Crystal structure of LpdA (Rv3303c) from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0050136 | molecular_function | NADH:ubiquinone reductase (non-electrogenic) activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 1990748 | biological_process | cellular detoxification |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0050136 | molecular_function | NADH:ubiquinone reductase (non-electrogenic) activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0070401 | molecular_function | NADP+ binding |
| B | 1990748 | biological_process | cellular detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A 999 |
| Chain | Residue |
| A | GLY9 |
| A | GLY41 |
| A | ALA42 |
| A | ALA43 |
| A | ASP47 |
| A | CYS48 |
| A | SER51 |
| A | LYS52 |
| A | GLY115 |
| A | ARG116 |
| A | GLY117 |
| A | GLY10 |
| A | ALA151 |
| A | THR152 |
| A | GLY153 |
| A | TRP172 |
| A | LEU284 |
| A | GLY316 |
| A | ASP317 |
| A | PRO323 |
| A | LEU324 |
| A | ALA325 |
| A | GLY11 |
| A | SER326 |
| A | PHE357 |
| A | HOH1015 |
| A | HOH1021 |
| B | TYR450 |
| B | HOH1049 |
| A | PRO12 |
| A | ALA13 |
| A | ILE34 |
| A | ASP35 |
| A | CYS36 |
| A | ASP37 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD B 999 |
| Chain | Residue |
| A | TYR450 |
| B | GLY9 |
| B | GLY11 |
| B | PRO12 |
| B | ALA13 |
| B | ILE34 |
| B | ASP35 |
| B | CYS36 |
| B | ASP37 |
| B | GLY41 |
| B | ALA42 |
| B | ALA43 |
| B | ASP47 |
| B | CYS48 |
| B | SER51 |
| B | LYS52 |
| B | ARG116 |
| B | GLY117 |
| B | ALA151 |
| B | THR152 |
| B | GLY153 |
| B | TRP172 |
| B | LEU284 |
| B | GLY316 |
| B | ASP317 |
| B | PRO323 |
| B | LEU324 |
| B | ALA325 |
| B | SER326 |
| B | PHE357 |
| B | HOH1024 |
| B | HOH1027 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15456792 |
| Chain | Residue | Details |
| A | PRO12 | |
| B | ASP35 | |
| B | ALA42 | |
| B | LYS52 | |
| B | GLY117 | |
| B | ASP317 | |
| B | LEU324 | |
| B | TYR450 | |
| A | ASP35 | |
| A | ALA42 | |
| A | LYS52 | |
| A | GLY117 | |
| A | ASP317 | |
| A | LEU324 | |
| A | TYR450 | |
| B | PRO12 |
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 | ALA43 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS48 | |
| B | ALA43 |
