6DEK
Crystal structure of Candida albicans acetohydroxyacid synthase catalytic subunit
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000463 | biological_process | maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| 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 | 0006412 | biological_process | translation |
| 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 | valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030150 | biological_process | protein import into mitochondrial matrix |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | ASP176 |
| A | LEU348 |
| A | GLY349 |
| A | MET350 |
| A | HIS351 |
| A | GLY370 |
| A | ALA371 |
| A | ARG372 |
| A | ASP374 |
| A | ARG376 |
| A | VAL377 |
| A | ARG237 |
| A | GLU403 |
| A | ILE404 |
| A | SER405 |
| A | ASN408 |
| A | GLY421 |
| A | ASP422 |
| A | VAL423 |
| A | MET498 |
| A | GLY516 |
| A | GLY517 |
| A | GLY303 |
| A | HOH819 |
| A | HOH825 |
| A | HOH841 |
| A | ALA304 |
| A | GLY305 |
| A | ASN308 |
| A | THR330 |
| A | LEU331 |
| A | GLN332 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 702 |
| Chain | Residue |
| A | GLN339 |
| A | ASP346 |
| A | GLN502 |
| A | PHE504 |
| A | HOH817 |
| A | HOH884 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 703 |
| Chain | Residue |
| A | ASP546 |
| A | ASN573 |
| A | GLU575 |
| A | TPP704 |
| A | HOH814 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue TPP A 704 |
| Chain | Residue |
| A | ALA110 |
| A | GLU135 |
| A | PRO161 |
| A | ASN165 |
| A | GLN198 |
| A | VAL493 |
| A | GLY494 |
| A | GLN495 |
| A | HIS496 |
| A | GLY519 |
| A | MET521 |
| A | GLY545 |
| A | ASP546 |
| A | ALA547 |
| A | SER548 |
| A | ASN573 |
| A | GLU575 |
| A | GLN576 |
| A | GLY577 |
| A | MET578 |
| A | VAL579 |
| A | MG703 |
| A | HOH814 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqvakPdaivIdIdGDAS |
| Chain | Residue | Details |
| A | ILE529-SER548 |
