6WO1
Hybrid acetohydroxyacid synthase complex structure with Cryptococcus neoformans AHAS catalytic subunit and Saccharomyces cerevisiae AHAS regulatory subunit
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003984 | molecular_function | acetolactate synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005948 | cellular_component | acetolactate synthase complex |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005948 | cellular_component | acetolactate synthase complex |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0030234 | molecular_function | enzyme regulator activity |
| B | 0042645 | cellular_component | mitochondrial nucleoid |
| B | 1990610 | molecular_function | acetolactate synthase regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue FAD A 1701 |
| Chain | Residue |
| A | ASP214 |
| A | ILE394 |
| A | GLY395 |
| A | MET396 |
| A | HIS397 |
| A | GLY416 |
| A | VAL417 |
| A | ARG418 |
| A | ASP420 |
| A | ARG422 |
| A | VAL423 |
| A | ARG275 |
| A | GLU449 |
| A | ILE450 |
| A | ASN454 |
| A | GLY467 |
| A | ASP468 |
| A | VAL469 |
| A | GLN543 |
| A | SER561 |
| A | GLY562 |
| A | GLY563 |
| A | GLY349 |
| A | ASN350 |
| A | GLY351 |
| A | SER354 |
| A | THR376 |
| A | LEU377 |
| A | GLN378 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue 8GF A 1702 |
| Chain | Residue |
| A | GLY565 |
| A | THR566 |
| A | MET567 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue DPO A 1703 |
| Chain | Residue |
| A | VAL539 |
| A | GLY540 |
| A | GLN541 |
| A | HIS542 |
| A | GLY591 |
| A | ASP592 |
| A | ALA593 |
| A | SER594 |
| A | MG1704 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 1704 |
| Chain | Residue |
| A | ASP592 |
| A | ASN619 |
| A | DPO1703 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue VAL B 401 |
| Chain | Residue |
| B | GLN85 |
| B | GLU87 |
| B | PRO88 |
| B | GLY89 |
| B | VAL90 |
| B | LEU91 |
| B | VAL110 |
| B | SER119 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGakvaaPekyvIdIdGDAS |
| Chain | Residue | Details |
| A | ILE575-SER594 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI4 |
| Number of Residues | 80 |
| Details | Domain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
