6UZI
Crystal structure of Dihydrolipoyl dehydrogenase from Elizabethkingia anophelis NUHP1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 | 0046872 | molecular_function | metal ion binding |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE9 |
| A | THR41 |
| A | CYS42 |
| A | VAL45 |
| A | GLY46 |
| A | CYS47 |
| A | SER50 |
| A | LYS51 |
| A | GLY113 |
| A | VAL114 |
| A | GLY115 |
| A | GLY10 |
| A | ALA143 |
| A | THR144 |
| A | GLY145 |
| A | SER146 |
| A | ILE185 |
| A | ARG273 |
| A | TYR276 |
| A | GLY312 |
| A | ASP313 |
| A | MET319 |
| A | SER11 |
| A | LEU320 |
| A | ALA321 |
| A | TYR352 |
| A | HOH607 |
| A | HOH608 |
| B | HIS445 |
| A | GLY12 |
| A | PRO13 |
| A | GLY14 |
| A | GLU33 |
| A | LYS34 |
| A | GLY40 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | HIS445 |
| A | GLU450 |
| B | GLU325 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | HIS466 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLY181 |
| A | GLY182 |
| A | LEU206 |
| A | HOH634 |
| C | GLY257 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | TYR205 |
| A | THR236 |
| A | VAL238 |
| A | HOH634 |
| C | ALA237 |
| C | SER239 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | MET391 |
| A | EDO507 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | TRP354 |
| A | PRO355 |
| A | ASP392 |
| A | ASP394 |
| A | ALA416 |
| A | EDO506 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 508 |
| Chain | Residue |
| A | GLU325 |
| B | HIS445 |
| B | GLU450 |
| site_id | AC9 |
| Number of Residues | 34 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| A | HIS445 |
| B | ILE9 |
| B | GLY10 |
| B | GLY12 |
| B | PRO13 |
| B | GLY14 |
| B | GLU33 |
| B | LYS34 |
| B | GLY40 |
| B | THR41 |
| B | CYS42 |
| B | VAL45 |
| B | GLY46 |
| B | CYS47 |
| B | SER50 |
| B | LYS51 |
| B | GLY113 |
| B | GLY115 |
| B | ALA143 |
| B | THR144 |
| B | GLY145 |
| B | SER146 |
| B | SER164 |
| B | ILE185 |
| B | ARG273 |
| B | TYR276 |
| B | LEU280 |
| B | GLY312 |
| B | ASP313 |
| B | MET319 |
| B | LEU320 |
| B | ALA321 |
| B | ALA324 |
| B | TYR352 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | HIS466 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | HOH619 |
| B | HOH622 |
| A | ARG417 |
| B | ASP55 |
| B | GLU58 |
| site_id | AD3 |
| Number of Residues | 32 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE9 |
| C | GLY10 |
| C | GLY12 |
| C | PRO13 |
| C | GLY14 |
| C | GLU33 |
| C | LYS34 |
| C | GLY40 |
| C | THR41 |
| C | CYS42 |
| C | GLY46 |
| C | CYS47 |
| C | SER50 |
| C | LYS51 |
| C | GLY113 |
| C | VAL114 |
| C | GLY115 |
| C | ALA143 |
| C | THR144 |
| C | GLY145 |
| C | SER146 |
| C | ILE185 |
| C | ARG273 |
| C | GLY312 |
| C | ASP313 |
| C | MET319 |
| C | LEU320 |
| C | ALA321 |
| C | HIS322 |
| C | TYR352 |
| D | HIS445 |
| D | PRO446 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | HIS445 |
| C | GLU450 |
| C | CL503 |
| D | GLU325 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | LEU384 |
| C | ZN502 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | GLY183 |
| C | VAL184 |
| C | ILE185 |
| C | SER270 |
| C | GLY272 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue ZN C 505 |
| Chain | Residue |
| C | GLU325 |
| D | HIS445 |
| D | GLU450 |
| site_id | AD8 |
| Number of Residues | 35 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS445 |
| D | ILE9 |
| D | GLY10 |
| D | SER11 |
| D | GLY12 |
| D | PRO13 |
| D | GLY14 |
| D | GLY15 |
| D | GLU33 |
| D | LYS34 |
| D | GLY40 |
| D | THR41 |
| D | CYS42 |
| D | VAL45 |
| D | GLY46 |
| D | CYS47 |
| D | SER50 |
| D | LYS51 |
| D | GLY113 |
| D | GLY115 |
| D | ALA143 |
| D | THR144 |
| D | GLY145 |
| D | SER146 |
| D | SER164 |
| D | ARG273 |
| D | TYR276 |
| D | GLY312 |
| D | ASP313 |
| D | MET319 |
| D | LEU320 |
| D | ALA321 |
| D | HIS322 |
| D | ALA324 |
| D | TYR352 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP |
| Chain | Residue | Details |
| A | GLY39-PRO49 |
