1EBD
DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 462 |
| Chain | Residue |
| A | GLY16 |
| A | CYS47 |
| A | VAL50 |
| A | GLY51 |
| A | CYS52 |
| A | LYS56 |
| A | GLY117 |
| A | GLU118 |
| A | ALA119 |
| A | ALA146 |
| A | THR147 |
| A | GLY18 |
| A | GLY148 |
| A | TYR186 |
| A | ILE187 |
| A | ARG274 |
| A | GLY313 |
| A | ASP314 |
| A | ALA320 |
| A | LEU321 |
| A | ALA322 |
| A | HOH470 |
| A | PRO19 |
| A | HOH478 |
| B | HIS446 |
| B | PRO447 |
| A | GLY20 |
| A | VAL38 |
| A | GLU39 |
| A | LYS40 |
| A | GLY45 |
| A | VAL46 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 462 |
| Chain | Residue |
| A | HIS446 |
| A | PRO447 |
| B | GLY16 |
| B | GLY18 |
| B | PRO19 |
| B | GLY20 |
| B | GLU39 |
| B | LYS40 |
| B | GLY45 |
| B | VAL46 |
| B | CYS47 |
| B | CYS52 |
| B | LYS56 |
| B | GLY117 |
| B | GLU118 |
| B | ALA119 |
| B | ALA146 |
| B | THR147 |
| B | GLY148 |
| B | TYR186 |
| B | ILE187 |
| B | ARG274 |
| B | GLY313 |
| B | ASP314 |
| B | ALA320 |
| B | LEU321 |
| B | ALA322 |
| B | HOH463 |
| B | HOH478 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8805537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 37 |
| Details | Domain: {"description":"Peripheral subunit-binding (PSBD)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01170","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU451 | |
| A | HIS446 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU451 | |
| B | HIS446 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS47 | |
| A | CYS52 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS47 | |
| B | CYS52 |
