6DEN
Crystal structure of Candida albicans acetohydroxyacid synthase in complex with the herbicide iodomuron ethyl
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 | 0005575 | cellular_component | cellular_component |
| 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 |
| A | 1901705 | biological_process | L-isoleucine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue K A 701 |
| Chain | Residue |
| A | GLN339 |
| A | ASP346 |
| A | GLN502 |
| A | PHE504 |
| A | HOH868 |
| A | HOH1334 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | TP9705 |
| A | HOH848 |
| A | ASP546 |
| A | ASN573 |
| A | GLU575 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue G8A A 703 |
| Chain | Residue |
| A | GLY112 |
| A | ALA113 |
| A | PRO188 |
| A | PHE197 |
| A | GLN198 |
| A | LYS247 |
| A | MET350 |
| A | ASP375 |
| A | ARG376 |
| A | MET578 |
| A | TRP582 |
| A | ALA653 |
| A | FAD704 |
| A | CO2706 |
| A | HOH908 |
| A | HOH938 |
| A | HOH1015 |
| A | HOH1178 |
| site_id | AC4 |
| Number of Residues | 38 |
| Details | binding site for residue FAD A 704 |
| Chain | Residue |
| A | ASP176 |
| A | PHE197 |
| A | ARG237 |
| A | GLY303 |
| A | ALA304 |
| A | GLY305 |
| A | ASN308 |
| A | THR330 |
| A | LEU331 |
| A | GLN332 |
| A | LEU348 |
| A | GLY349 |
| A | MET350 |
| A | HIS351 |
| A | GLY370 |
| A | ALA371 |
| A | ARG372 |
| A | ASP374 |
| A | ARG376 |
| A | VAL377 |
| A | GLU403 |
| A | ILE404 |
| A | ASN408 |
| A | GLY421 |
| A | ASP422 |
| A | VAL423 |
| A | GLN497 |
| A | MET498 |
| A | SER515 |
| A | GLY516 |
| A | GLY517 |
| A | MET578 |
| A | G8A703 |
| A | HOH827 |
| A | HOH914 |
| A | HOH940 |
| A | HOH947 |
| A | HOH1248 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue TP9 A 705 |
| Chain | Residue |
| A | ALA110 |
| A | GLY111 |
| 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 | MG702 |
| A | CO2706 |
| A | HOH848 |
| A | HOH851 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CO2 A 706 |
| Chain | Residue |
| A | HOH1026 |
| A | GLN198 |
| A | VAL493 |
| A | MET578 |
| A | G8A703 |
| A | TP9705 |
| A | HOH938 |
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 |
