5Y8L
Mycobacterium tuberculosis 3-Hydroxyisobutyrate dehydrogenase (MtHIBADH) + NAD +(S)-3-hydroxyisobutyrate (S-HIBA)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006574 | biological_process | valine catabolic process |
| A | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| 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 | 0006574 | biological_process | valine catabolic process |
| B | 0008442 | molecular_function | 3-hydroxyisobutyrate dehydrogenase activity |
| B | 0009083 | biological_process | branched-chain amino acid catabolic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY8 |
| A | VAL70 |
| A | THR93 |
| A | VAL118 |
| A | GLY121 |
| A | LYS168 |
| A | LEU240 |
| A | LYS243 |
| A | HOH418 |
| A | HOH428 |
| A | HOH439 |
| A | GLY10 |
| A | HOH447 |
| A | HOH450 |
| A | HOH463 |
| A | HOH481 |
| A | HOH503 |
| A | HOH552 |
| A | HOH564 |
| A | HOH580 |
| A | HOH603 |
| A | ASN11 |
| A | MET12 |
| A | PHE30 |
| A | ASP31 |
| A | PRO32 |
| A | MET64 |
| A | LEU65 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | ALA58 |
| A | ASP59 |
| A | ARG83 |
| A | PRO84 |
| A | ALA85 |
| A | THR86 |
| A | ARG143 |
| A | HOH426 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | HIS25 |
| A | VAL26 |
| A | VAL27 |
| A | GLY44 |
| A | THR76 |
| A | LEU79 |
| A | ALA80 |
| A | HOH406 |
| A | HOH500 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | SER119 |
| A | ASN172 |
| A | PHE236 |
| A | HOH405 |
| A | HOH408 |
| A | HOH576 |
| B | HOH411 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue 9ON A 305 |
| Chain | Residue |
| A | ARG145 |
| A | GLU149 |
| A | ALA152 |
| A | GLY153 |
| A | ILE155 |
| A | HOH401 |
| A | HOH407 |
| A | HOH409 |
| A | HOH590 |
| A | HOH703 |
| B | ALA254 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY8 |
| B | GLY10 |
| B | ASN11 |
| B | MET12 |
| B | PHE30 |
| B | ASP31 |
| B | PRO32 |
| B | ALA33 |
| B | MET64 |
| B | LEU65 |
| B | PRO66 |
| B | VAL70 |
| B | THR93 |
| B | VAL118 |
| B | GLY121 |
| B | LYS168 |
| B | LEU240 |
| B | LYS243 |
| B | HOH422 |
| B | HOH425 |
| B | HOH438 |
| B | HOH444 |
| B | HOH470 |
| B | HOH471 |
| B | HOH479 |
| B | HOH491 |
| B | HOH492 |
| B | HOH510 |
| B | HOH525 |
| B | HOH577 |
| B | HOH585 |
| B | HOH601 |
| B | HOH624 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue HUI B 302 |
| Chain | Residue |
| B | SER119 |
| B | GLY120 |
| B | TRP211 |
| B | PHE236 |
| B | HOH474 |
| B | HOH627 |
| A | THR207 |
| A | ASP275 |
| A | HOH520 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ALA41 |
| B | ALA58 |
| B | ASP59 |
| B | ARG83 |
| B | PRO84 |
| B | THR86 |
| B | HOH459 |
| B | HOH516 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue 9ON B 304 |
| Chain | Residue |
| B | GLU149 |
| B | ALA152 |
| B | GLY153 |
| B | LYS154 |
| B | HOH408 |
| B | HOH556 |
| B | HOH614 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue 9ON B 305 |
| Chain | Residue |
| A | ALA270 |
| A | LYS271 |
| A | ALA274 |
| B | THR129 |
| B | LEU130 |
| B | ALA131 |
| B | GLY153 |
| B | LYS154 |
| B | HOH466 |
| B | HOH602 |
Functional Information from PROSITE/UniProt
| site_id | PS00895 |
| Number of Residues | 14 |
| Details | 3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FLGLGnMGapMSaN |
| Chain | Residue | Details |
| A | PHE6-ASN19 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS168 | |
| B | LYS168 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR3 | |
| A | THR93 | |
| A | LYS243 | |
| B | THR3 | |
| B | THR93 | |
| B | LYS243 |
