3WWH
Crystal structure of the first R-stereoselective -transaminase identified from Arthrobacter sp. KNK168 (FERM-BP-5228)
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 | 0005829 | cellular_component | cytosol |
A | 0006532 | biological_process | aspartate biosynthetic process |
A | 0009098 | biological_process | L-leucine biosynthetic process |
A | 0009099 | biological_process | valine biosynthetic process |
A | 0046394 | biological_process | carboxylic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 401 |
Chain | Residue |
A | ARG86 |
A | THR283 |
A | GOL402 |
A | HOH503 |
A | HOH554 |
A | HOH706 |
A | LYS188 |
A | GLU221 |
A | PHE225 |
A | LEU243 |
A | GLY245 |
A | ILE246 |
A | THR247 |
A | THR282 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | HIS62 |
A | TYR67 |
A | VAL69 |
A | ARG138 |
A | LYS188 |
A | PLP401 |
A | HOH556 |