5JE8
The crystal structure of Bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| A | 0016054 | biological_process | organic acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| B | 0016054 | biological_process | organic acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| C | 0016054 | biological_process | organic acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| D | 0016054 | biological_process | organic acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY10 |
| A | VAL74 |
| A | SER95 |
| A | THR96 |
| A | VAL121 |
| A | GLY124 |
| A | PHE234 |
| A | LEU238 |
| A | EPE402 |
| A | HOH510 |
| A | HOH518 |
| A | ASN11 |
| A | HOH541 |
| A | HOH574 |
| A | HOH580 |
| A | HOH593 |
| A | HOH596 |
| A | HOH599 |
| A | HOH601 |
| A | HOH602 |
| A | HOH603 |
| A | MET12 |
| A | ASP31 |
| A | LEU32 |
| A | SER64 |
| A | LEU65 |
| A | PRO66 |
| A | ALA70 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue EPE A 402 |
| Chain | Residue |
| A | SER122 |
| A | GLY123 |
| A | GLY124 |
| A | ILE126 |
| A | LYS172 |
| A | ASN176 |
| A | ILE179 |
| A | ARG219 |
| A | PHE234 |
| A | NAD401 |
| A | HOH508 |
| A | HOH514 |
| A | HOH617 |
| B | TYR211 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY8 |
| B | GLY10 |
| B | ASN11 |
| B | MET12 |
| B | ASP31 |
| B | LEU32 |
| B | SER64 |
| B | LEU65 |
| B | PRO66 |
| B | VAL74 |
| B | SER95 |
| B | THR96 |
| B | VAL121 |
| B | GLY124 |
| B | LEU238 |
| B | HOH502 |
| B | HOH507 |
| B | HOH508 |
| B | HOH517 |
| B | HOH538 |
| B | HOH547 |
| B | HOH570 |
| B | HOH577 |
| B | HOH642 |
| D | GLN272 |
| D | ALA273 |
| D | HOH521 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | ASP268 |
| B | SER271 |
| B | GLN272 |
| B | HOH522 |
| B | HOH554 |
| B | HOH597 |
| D | ASN237 |
| D | LYS241 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| C | GLY8 |
| C | GLY10 |
| C | ASN11 |
| C | MET12 |
| C | ASP31 |
| C | LEU32 |
| C | LEU65 |
| C | PRO66 |
| C | VAL74 |
| C | THR96 |
| C | VAL121 |
| C | GLY124 |
| C | LEU238 |
| C | HOH511 |
| C | HOH528 |
| C | HOH538 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| D | LEU32 |
| D | LEU65 |
| D | PRO66 |
| D | SER95 |
| D | THR96 |
| D | VAL121 |
| D | LEU238 |
| D | HOH502 |
| D | HOH506 |
| D | HOH524 |
| D | HOH562 |
| B | ALA273 |
| B | HOH535 |
| D | GLY10 |
| D | ASN11 |
| D | MET12 |
| D | ASP31 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| B | ASN237 |
| B | LYS241 |
| B | HOH552 |
| D | ASP268 |
| D | SER271 |
| D | GLN272 |
| D | HOH512 |
| D | HOH533 |
Functional Information from PROSITE/UniProt
| site_id | PS00895 |
| Number of Residues | 14 |
| Details | 3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGnMGlpMSkN |
| Chain | Residue | Details |
| A | PHE6-ASN19 |
