2EQ9
Crystal structure of lipoamide dehydrogenase from thermus thermophilus HB8 with psbdb
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 (NADH) activity |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 (NADH) activity |
| D | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 (NADH) activity |
| E | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| G | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| H | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| I | 0016746 | molecular_function | acyltransferase activity |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| J | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| K | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| L | 0016746 | molecular_function | acyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 8482 |
| 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 | LEU281 |
| A | GLY313 |
| A | ASP314 |
| A | LEU320 |
| A | LEU321 |
| A | ALA322 |
| A | HIS323 |
| A | GLY18 |
| A | ALA325 |
| A | TYR353 |
| A | HOH8484 |
| A | HOH8487 |
| A | HOH8491 |
| A | HOH8498 |
| A | HOH8507 |
| A | HOH8564 |
| B | HIS446 |
| A | PRO19 |
| A | GLY20 |
| A | GLU39 |
| A | ALA40 |
| A | GLU42 |
| A | GLY45 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD B 1482 |
| 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 | LEU281 |
| B | GLY313 |
| B | ASP314 |
| B | LEU320 |
| B | LEU321 |
| B | ALA322 |
| B | HIS323 |
| B | TYR353 |
| B | HOH1503 |
| B | HOH1504 |
| B | HOH1512 |
| B | HOH1529 |
| B | HOH1530 |
| B | HOH1584 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD D 2482 |
| Chain | Residue |
| D | GLY313 |
| D | ASP314 |
| D | LEU320 |
| D | LEU321 |
| D | ALA322 |
| D | HIS323 |
| D | TYR353 |
| D | HOH2491 |
| D | HOH2493 |
| D | HOH2496 |
| D | HOH2503 |
| D | HOH2504 |
| D | HOH2575 |
| 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 |
| D | THR147 |
| D | GLY148 |
| D | SER166 |
| D | ARG274 |
| D | ARG277 |
| D | LEU281 |
| site_id | AC4 |
| Number of Residues | 38 |
| 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 | LEU281 |
| E | GLY313 |
| E | ASP314 |
| E | LEU320 |
| E | LEU321 |
| E | ALA322 |
| E | HIS323 |
| E | TYR353 |
| E | HOH3491 |
| E | HOH3503 |
| E | HOH3508 |
| E | HOH3514 |
| E | HOH3522 |
| E | HOH3585 |
| site_id | AC5 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD G 4482 |
| Chain | Residue |
| G | ILE15 |
| G | GLY16 |
| G | GLY18 |
| G | PRO19 |
| G | GLY20 |
| G | GLU39 |
| G | ALA40 |
| G | GLU42 |
| G | GLY45 |
| G | CYS47 |
| G | GLY51 |
| G | CYS52 |
| G | LYS56 |
| G | GLY117 |
| G | PHE118 |
| G | ALA119 |
| G | ALA146 |
| G | THR147 |
| G | GLY148 |
| G | SER166 |
| G | ARG274 |
| G | LEU281 |
| G | GLY313 |
| G | ASP314 |
| G | LEU320 |
| G | LEU321 |
| G | ALA322 |
| G | HIS323 |
| G | TYR353 |
| G | HOH4492 |
| G | HOH4502 |
| G | HOH4511 |
| G | HOH4572 |
| G | HOH4598 |
| G | HOH4607 |
| H | HIS446 |
| site_id | AC6 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD H 5482 |
| Chain | Residue |
| G | HIS446 |
| H | ILE15 |
| H | GLY16 |
| H | GLY18 |
| H | PRO19 |
| H | GLY20 |
| H | GLU39 |
| H | ALA40 |
| H | GLU42 |
| H | GLY45 |
| H | CYS47 |
| H | GLY51 |
| H | CYS52 |
| H | THR55 |
| H | LYS56 |
| H | GLY117 |
| H | PHE118 |
| H | ALA119 |
| H | ALA146 |
| H | THR147 |
| H | GLY148 |
| H | SER166 |
| H | ARG274 |
| H | ARG277 |
| H | LEU281 |
| H | GLY313 |
| H | ASP314 |
| H | LEU320 |
| H | LEU321 |
| H | ALA322 |
| H | HIS323 |
| H | TYR353 |
| H | HOH5483 |
| H | HOH5485 |
| H | HOH5493 |
| H | HOH5501 |
| H | HOH5506 |
| H | HOH5555 |
| H | HOH5593 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD J 6482 |
| Chain | Residue |
| J | ILE15 |
| J | GLY16 |
| J | GLY18 |
| J | PRO19 |
| J | GLY20 |
| J | GLY21 |
| J | GLU39 |
| J | ALA40 |
| J | GLU42 |
| J | GLY45 |
| J | CYS47 |
| J | GLY51 |
| J | CYS52 |
| J | THR55 |
| J | LYS56 |
| J | GLY117 |
| J | PHE118 |
| J | ALA119 |
| J | ALA146 |
| J | THR147 |
| J | GLY148 |
| J | SER166 |
| J | ARG274 |
| J | LEU281 |
| J | GLY313 |
| J | ASP314 |
| J | LEU320 |
| J | LEU321 |
| J | ALA322 |
| J | HIS323 |
| J | TYR353 |
| J | HOH6495 |
| J | HOH6496 |
| J | HOH6516 |
| J | HOH6524 |
| J | HOH6528 |
| K | HIS446 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD K 7482 |
| Chain | Residue |
| J | HIS446 |
| K | ILE15 |
| K | GLY16 |
| K | GLY18 |
| K | PRO19 |
| K | GLY20 |
| K | GLU39 |
| K | ALA40 |
| K | GLU42 |
| K | GLY45 |
| K | CYS47 |
| K | GLY51 |
| K | CYS52 |
| K | THR55 |
| K | LYS56 |
| K | PHE118 |
| K | ALA119 |
| K | ALA146 |
| K | THR147 |
| K | GLY148 |
| K | SER166 |
| K | ARG274 |
| K | ARG277 |
| K | LEU281 |
| K | GLY313 |
| K | ASP314 |
| K | LEU320 |
| K | LEU321 |
| K | ALA322 |
| K | HIS323 |
| K | TYR353 |
| K | HOH7487 |
| K | HOH7489 |
| K | HOH7523 |
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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU451 | |
| B | HIS446 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | GLU451 | |
| D | HIS446 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| E | GLU451 | |
| E | HIS446 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| G | GLU451 | |
| G | HIS446 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| H | GLU451 | |
| H | HIS446 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| J | GLU451 | |
| J | HIS446 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| K | GLU451 | |
| K | HIS446 |
| 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 |
| G | CYS47 | |
| G | CYS52 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| H | CYS47 | |
| H | CYS52 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| J | CYS47 | |
| J | CYS52 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| K | CYS47 | |
| K | CYS52 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU451 | |
| A | HIS446 |
