Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009436 | biological_process | glyoxylate catabolic process |
A | 0019481 | biological_process | L-alanine catabolic process, by transamination |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue 7F7 A 501 |
Chain | Residue |
A | LEU19 |
A | VAL240 |
A | LYS241 |
A | LYS267 |
A | GLN294 |
A | THR295 |
A | TRP436 |
A | HOH643 |
A | HOH670 |
A | HOH677 |
A | HOH838 |
A | TRP49 |
A | SER109 |
A | GLY110 |
A | SER111 |
A | TYR137 |
A | HIS138 |
A | GLU205 |
A | ASP238 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | ARG33 |
A | ARG123 |
A | ASP155 |
A | HOH623 |
A | HOH757 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VVcDEVkv.GLaRsGrlhcfehegfvp....DILvlGKglgGG |
Chain | Residue | Details |
A | VAL235-GLY272 | |