6HNU
Crystal structure of the aminotransferase Aro8 from C. Albicans with ligands
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006571 | biological_process | L-tyrosine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008793 | molecular_function | aromatic-amino-acid transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009074 | biological_process | aromatic amino acid family catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006571 | biological_process | L-tyrosine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008793 | molecular_function | aromatic-amino-acid transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009074 | biological_process | aromatic amino acid family catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue BTB A 501 |
| Chain | Residue |
| A | TYR164 |
| A | HOH657 |
| A | HOH695 |
| A | HOH761 |
| A | HOH869 |
| A | ASP186 |
| A | GLU187 |
| A | THR220 |
| A | THR395 |
| A | THR397 |
| A | LYS457 |
| A | PHE461 |
| A | HOH650 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | SER222 |
| A | SER223 |
| A | ASN386 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | TYR164 |
| A | HOH1041 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue BTB B 501 |
| Chain | Residue |
| B | TYR164 |
| B | MET185 |
| B | ASP186 |
| B | GLU187 |
| B | THR220 |
| B | THR395 |
| B | THR397 |
| B | LYS457 |
| B | PHE461 |
| B | HOH626 |
| B | HOH669 |
| B | HOH723 |
| B | HOH754 |
| B | HOH801 |
| B | HOH803 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue TRS B 504 |
| Chain | Residue |
| A | LYS415 |
| B | GLN116 |
| B | GLU120 |
| B | ARG345 |
| B | HOH620 |
| B | HOH978 |
| B | HOH990 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | SER222 |
| B | SER223 |
| B | ASN386 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | TYR164 |
| B | HOH1058 |
| B | HOH1064 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide PLP A 502 and PHE A 503 |
| Chain | Residue |
| A | GLY140 |
| A | ASN141 |
| A | THR142 |
| A | PHE166 |
| A | ILE213 |
| A | ASN218 |
| A | ASP246 |
| A | TYR249 |
| A | SER297 |
| A | SER299 |
| A | LYS300 |
| A | ARG307 |
| B | TYR105 |
| B | HOH809 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP B 502 and PHE B 503 |
| Chain | Residue |
| A | LEU47 |
| A | TYR105 |
| A | GLN330 |
| A | HOH675 |
| B | GLY140 |
| B | ASN141 |
| B | THR142 |
| B | PHE166 |
| B | TYR211 |
| B | ILE213 |
| B | ASN218 |
| B | ASP246 |
| B | TYR249 |
| B | SER297 |
| B | SER299 |
| B | LYS300 |
| B | ARG307 |
| B | HOH850 |
| B | HOH964 |
