6DEL
Crystal structure of Candida albicans acetohydroxyacid synthase in complex with the herbicide chlorimuron ethyl
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 | 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 | 6 |
Details | binding site for residue K A 701 |
Chain | Residue |
A | GLN339 |
A | ASP346 |
A | GLN502 |
A | PHE504 |
A | HOH869 |
A | HOH1228 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 702 |
Chain | Residue |
A | TP9705 |
A | G8G706 |
A | HOH887 |
A | ASP546 |
A | ASN573 |
A | GLU575 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue CIE 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 | FMT707 |
A | HOH832 |
site_id | AC4 |
Number of Residues | 37 |
Details | binding site for residue FAD A 704 |
Chain | Residue |
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 | GLY516 |
A | GLY517 |
A | MET578 |
A | CIE703 |
A | HOH801 |
A | HOH806 |
A | HOH877 |
A | HOH894 |
A | HOH939 |
A | HOH1147 |
site_id | AC5 |
Number of Residues | 26 |
Details | binding site for residue TP9 A 705 |
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 | MG702 |
A | G8G706 |
A | FMT707 |
A | HOH887 |
A | HOH1073 |
site_id | AC6 |
Number of Residues | 28 |
Details | binding site for residue G8G A 706 |
Chain | Residue |
A | HIS496 |
A | GLY519 |
A | MET521 |
A | GLY545 |
A | ASP546 |
A | ALA547 |
A | SER548 |
A | MET551 |
A | ASN573 |
A | GLU575 |
A | GLN576 |
A | GLY577 |
A | MET578 |
A | VAL579 |
A | MG702 |
A | TP9705 |
A | FMT707 |
A | HOH887 |
A | HOH1073 |
A | ALA110 |
A | GLY111 |
A | GLU135 |
A | PRO161 |
A | ASN165 |
A | GLN198 |
A | VAL493 |
A | GLY494 |
A | GLN495 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue FMT A 707 |
Chain | Residue |
A | GLY112 |
A | GLN198 |
A | CIE703 |
A | TP9705 |
A | G8G706 |
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 |