4WHX
X-ray Crystal Structure of an Amino Acid Aminotransferase from Burkholderia pseudomallei Bound to the Co-factor Pyridoxal Phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| B | 0009081 | biological_process | branched-chain amino acid metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| C | 0009081 | biological_process | branched-chain amino acid metabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| D | 0009081 | biological_process | branched-chain amino acid metabolic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| E | 0009081 | biological_process | branched-chain amino acid metabolic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| F | 0009081 | biological_process | branched-chain amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ALA A 401 |
| Chain | Residue |
| A | TYR98 |
| A | LLP161 |
| A | GLY198 |
| A | THR258 |
| A | ALA259 |
| A | HOH679 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | TYR131 |
| A | ASN173 |
| A | HOH617 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue ALA C 401 |
| Chain | Residue |
| C | GLY40 |
| C | TYR98 |
| C | LLP161 |
| C | GLY198 |
| C | THR258 |
| C | ALA259 |
| C | HOH517 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ALA D 401 |
| Chain | Residue |
| D | PHE38 |
| D | TYR98 |
| D | LLP161 |
| D | THR258 |
| D | ALA259 |
| D | HOH548 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue ALA E 401 |
| Chain | Residue |
| E | GLY40 |
| E | TYR98 |
| E | LLP161 |
| E | GLY198 |
| E | THR258 |
| E | ALA259 |
| E | HOH636 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 402 |
| Chain | Residue |
| E | ARG42 |
| E | TYR44 |
| E | GLU261 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 29 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSgeNFFlvnrgk......LyTpdlasc..LdGItR |
| Chain | Residue | Details |
| A | GLU195-ARG223 |
