6BZ0
1.83 Angstrom Resolution Crystal Structure of Dihydrolipoyl Dehydrogenase from Acinetobacter baumannii in Complex with FAD.
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 | 0000166 | molecular_function | nucleotide binding |
| C | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 41 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | GLY46 |
| A | THR47 |
| A | CYS48 |
| A | GLY52 |
| A | CYS53 |
| A | LYS57 |
| A | GLY119 |
| A | THR120 |
| A | GLY121 |
| A | ALA149 |
| A | GLY11 |
| A | SER150 |
| A | GLY151 |
| A | SER152 |
| A | SER170 |
| A | ILE191 |
| A | ARG278 |
| A | TYR281 |
| A | GLY317 |
| A | ASP318 |
| A | MET324 |
| A | GLY13 |
| A | LEU325 |
| A | ALA326 |
| A | HIS327 |
| A | ALA329 |
| A | TYR357 |
| A | HOH648 |
| A | HOH657 |
| A | HOH663 |
| A | HOH669 |
| A | HOH713 |
| A | PRO14 |
| B | HIS450 |
| B | HOH686 |
| A | GLY15 |
| A | ILE33 |
| A | GLU34 |
| A | LYS35 |
| A | ARG36 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | SER170 |
| A | ARG278 |
| A | HOH732 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | VAL168 |
| A | ASP169 |
| A | GLY172 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | LYS221 |
| A | GLU370 |
| A | HOH676 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | HOH731 |
| A | HOH748 |
| A | HOH920 |
| D | HOH635 |
| D | HOH881 |
| D | HOH888 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 506 |
| Chain | Residue |
| A | HOH641 |
| A | HOH838 |
| A | HOH860 |
| A | HOH915 |
| A | HOH918 |
| A | HOH937 |
| site_id | AC7 |
| Number of Residues | 39 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | HOH650 |
| B | HOH705 |
| A | HIS450 |
| A | HOH753 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | PRO14 |
| B | GLY15 |
| B | ILE33 |
| B | GLU34 |
| B | LYS35 |
| B | ARG36 |
| B | GLY46 |
| B | THR47 |
| B | CYS48 |
| B | GLY52 |
| B | CYS53 |
| B | LYS57 |
| B | GLY119 |
| B | THR120 |
| B | GLY121 |
| B | ALA149 |
| B | SER150 |
| B | GLY151 |
| B | SER152 |
| B | SER170 |
| B | ILE191 |
| B | ARG278 |
| B | TYR281 |
| B | GLY317 |
| B | ASP318 |
| B | MET324 |
| B | LEU325 |
| B | ALA326 |
| B | HIS327 |
| B | ALA329 |
| B | TYR357 |
| B | HOH637 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | LEU216 |
| B | PRO217 |
| B | MET218 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | GLU296 |
| B | ARG297 |
| B | GLY298 |
| B | HOH625 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | ASP220 |
| B | LYS221 |
| B | GLU370 |
| site_id | AD2 |
| Number of Residues | 39 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE10 |
| C | GLY11 |
| C | GLY13 |
| C | PRO14 |
| C | GLY15 |
| C | ILE33 |
| C | GLU34 |
| C | LYS35 |
| C | ARG36 |
| C | GLY46 |
| C | THR47 |
| C | CYS48 |
| C | GLY52 |
| C | CYS53 |
| C | LYS57 |
| C | GLY119 |
| C | THR120 |
| C | GLY121 |
| C | ALA149 |
| C | SER150 |
| C | GLY151 |
| C | SER152 |
| C | SER170 |
| C | ILE191 |
| C | ARG278 |
| C | TYR281 |
| C | GLY317 |
| C | ASP318 |
| C | MET324 |
| C | LEU325 |
| C | ALA326 |
| C | TYR357 |
| C | HOH641 |
| C | HOH649 |
| C | HOH657 |
| C | HOH666 |
| C | HOH727 |
| D | HIS450 |
| D | HOH676 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | SER170 |
| C | ILE191 |
| C | ARG278 |
| C | HOH707 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | VAL162 |
| C | GLN164 |
| C | ASP169 |
| C | GLY172 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 504 |
| Chain | Residue |
| C | MET218 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 505 |
| Chain | Residue |
| C | LYS221 |
| C | GLU370 |
| C | HOH724 |
| site_id | AD7 |
| Number of Residues | 40 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS450 |
| C | HOH684 |
| D | ILE10 |
| D | GLY11 |
| D | GLY13 |
| D | PRO14 |
| D | GLY15 |
| D | GLU34 |
| D | LYS35 |
| D | ARG36 |
| D | GLY46 |
| D | THR47 |
| D | CYS48 |
| D | GLY52 |
| D | CYS53 |
| D | LYS57 |
| D | GLY119 |
| D | THR120 |
| D | GLY121 |
| D | ALA149 |
| D | SER150 |
| D | GLY151 |
| D | SER152 |
| D | SER170 |
| D | ILE191 |
| D | ARG278 |
| D | TYR281 |
| D | GLY317 |
| D | ASP318 |
| D | MET324 |
| D | LEU325 |
| D | ALA326 |
| D | HIS327 |
| D | ALA329 |
| D | TYR357 |
| D | HOH606 |
| D | HOH703 |
| D | HOH704 |
| D | HOH709 |
| D | HOH727 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 502 |
| Chain | Residue |
| D | LYS221 |
| D | GLU370 |
| D | HOH790 |
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 | GLY45-PRO55 |
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNDhCATSVeGVyaigdlV |
| Chain | Residue | Details |
| A | VAL302-VAL320 |
