2EQ8
Crystal structure of lipoamide dehydrogenase from thermus thermophilus HB8 with psbdp
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0016746 | molecular_function | acyltransferase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0016746 | molecular_function | acyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD A 4482 |
| Chain | Residue |
| A | ILE15 |
| A | CYS47 |
| A | GLY51 |
| A | CYS52 |
| A | THR55 |
| A | LYS56 |
| A | GLY117 |
| A | PHE118 |
| A | ALA119 |
| A | ALA146 |
| A | THR147 |
| A | GLY16 |
| A | GLY148 |
| A | SER166 |
| A | ARG274 |
| A | ARG277 |
| A | LEU281 |
| A | GLY313 |
| A | ASP314 |
| A | LEU320 |
| A | LEU321 |
| A | ALA322 |
| A | GLY18 |
| A | HIS323 |
| A | TYR353 |
| A | HOH4483 |
| A | HOH4484 |
| A | HOH4494 |
| A | HOH4503 |
| A | HOH4505 |
| A | HOH4506 |
| A | HOH4523 |
| A | HOH4540 |
| A | PRO19 |
| A | HOH4804 |
| B | HIS446 |
| A | GLY20 |
| A | GLU39 |
| A | ALA40 |
| A | GLU42 |
| A | GLY45 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 5482 |
| Chain | Residue |
| A | HIS446 |
| B | ILE15 |
| B | GLY16 |
| B | GLY18 |
| B | PRO19 |
| B | GLY20 |
| B | GLU39 |
| B | ALA40 |
| B | GLU42 |
| B | GLY45 |
| B | CYS47 |
| B | GLY51 |
| B | CYS52 |
| B | THR55 |
| B | LYS56 |
| B | GLY117 |
| B | PHE118 |
| B | ALA119 |
| B | ALA146 |
| B | THR147 |
| B | GLY148 |
| B | SER166 |
| B | ARG274 |
| B | ARG277 |
| B | GLY313 |
| B | ASP314 |
| B | LEU320 |
| B | LEU321 |
| B | ALA322 |
| B | HIS323 |
| B | ALA325 |
| B | TYR353 |
| B | HOH5484 |
| B | HOH5490 |
| B | HOH5492 |
| B | HOH5516 |
| B | HOH5525 |
| B | HOH5559 |
| B | HOH5596 |
| B | HOH5771 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD D 2482 |
| Chain | Residue |
| D | THR147 |
| D | GLY148 |
| D | SER166 |
| D | ARG274 |
| D | ARG277 |
| D | GLY313 |
| D | ASP314 |
| D | LEU320 |
| D | LEU321 |
| D | ALA322 |
| D | HIS323 |
| D | TYR353 |
| D | HOH2486 |
| D | HOH2491 |
| D | HOH2502 |
| D | HOH2504 |
| D | HOH2507 |
| D | HOH2508 |
| D | HOH2512 |
| D | HOH2658 |
| E | HIS446 |
| D | ILE15 |
| D | GLY16 |
| D | GLY18 |
| D | PRO19 |
| D | GLY20 |
| D | GLU39 |
| D | ALA40 |
| D | GLU42 |
| D | GLY45 |
| D | CYS47 |
| D | GLY51 |
| D | CYS52 |
| D | THR55 |
| D | LYS56 |
| D | GLY117 |
| D | PHE118 |
| D | ALA119 |
| D | ALA146 |
| site_id | AC4 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD E 3482 |
| Chain | Residue |
| D | HIS446 |
| E | ILE15 |
| E | GLY16 |
| E | GLY18 |
| E | PRO19 |
| E | GLY20 |
| E | GLU39 |
| E | ALA40 |
| E | GLU42 |
| E | GLY45 |
| E | CYS47 |
| E | GLY51 |
| E | CYS52 |
| E | THR55 |
| E | LYS56 |
| E | GLY117 |
| E | PHE118 |
| E | ALA119 |
| E | ALA146 |
| E | THR147 |
| E | GLY148 |
| E | SER166 |
| E | ARG274 |
| E | ARG277 |
| E | GLY313 |
| E | ASP314 |
| E | LEU320 |
| E | LEU321 |
| E | ALA322 |
| E | HIS323 |
| E | ALA325 |
| E | TYR353 |
| E | HOH3484 |
| E | HOH3486 |
| E | HOH3490 |
| E | HOH3499 |
| E | HOH3545 |
| E | HOH3556 |
| E | HOH3625 |
| E | HOH3644 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP |
| Chain | Residue | Details |
| A | GLY44-PRO54 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS47 | |
| A | CYS52 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS47 | |
| B | CYS52 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | CYS47 | |
| D | CYS52 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| E | CYS47 | |
| E | CYS52 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU451 | |
| A | HIS446 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU451 | |
| B | HIS446 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | GLU451 | |
| D | HIS446 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| E | GLU451 | |
| E | HIS446 |
