6CUZ
Engineered TrpB from Pyrococcus furiosus, PfTrpB7E6 with (2S,3R)-ethylserine bound as the amino-acrylate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0004834 | molecular_function | tryptophan synthase activity |
| A | 0006568 | biological_process | tryptophan metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000162 | biological_process | tryptophan biosynthetic process |
| B | 0004834 | molecular_function | tryptophan synthase activity |
| B | 0006568 | biological_process | tryptophan metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000162 | biological_process | tryptophan biosynthetic process |
| C | 0004834 | molecular_function | tryptophan synthase activity |
| C | 0006568 | biological_process | tryptophan metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0000162 | biological_process | tryptophan biosynthetic process |
| D | 0004834 | molecular_function | tryptophan synthase activity |
| D | 0006568 | biological_process | tryptophan metabolic process |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 401 |
| Chain | Residue |
| A | GLY227 |
| A | SER263 |
| A | SER265 |
| A | TYR301 |
| A | GLY303 |
| A | HOH531 |
| A | HOH566 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | HOH618 |
| B | GLY48 |
| B | PRO50 |
| B | HOH607 |
| A | GLY48 |
| A | PRO50 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue FEV A 403 |
| Chain | Residue |
| A | HIS81 |
| A | LYS82 |
| A | THR105 |
| A | GLY106 |
| A | ALA107 |
| A | GLY108 |
| A | GLN109 |
| A | HIS110 |
| A | SER185 |
| A | GLY227 |
| A | GLY228 |
| A | GLY229 |
| A | SER230 |
| A | ASN231 |
| A | GLY298 |
| A | GLU345 |
| A | SER371 |
| A | HOH529 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 401 |
| Chain | Residue |
| B | GLY227 |
| B | SER263 |
| B | SER265 |
| B | TYR301 |
| B | GLY303 |
| B | HOH584 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 401 |
| Chain | Residue |
| C | SER263 |
| C | SER265 |
| C | TYR301 |
| C | GLY303 |
| C | HOH555 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 C 402 |
| Chain | Residue |
| C | LLP82 |
| C | THR105 |
| C | GLY106 |
| C | ALA107 |
| C | GLY108 |
| C | GLN109 |
| C | HIS110 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue NA D 401 |
| Chain | Residue |
| D | GLY227 |
| D | SER263 |
| D | SER265 |
| D | TYR301 |
| D | GLY303 |
| D | HOH513 |
| D | HOH566 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 402 |
| Chain | Residue |
| C | GLY48 |
| C | PRO50 |
| C | HOH620 |
| D | GLY48 |
| D | PRO50 |
| D | HOH633 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for residue FEV D 403 |
| Chain | Residue |
| D | HIS81 |
| D | LYS82 |
| D | THR105 |
| D | GLY106 |
| D | ALA107 |
| D | GLY108 |
| D | GLN109 |
| D | HIS110 |
| D | ALA161 |
| D | SER185 |
| D | GLY227 |
| D | GLY228 |
| D | GLY229 |
| D | SER230 |
| D | ASN231 |
| D | GLY298 |
| D | GLU345 |
| D | SER371 |
| D | HOH554 |
Functional Information from PROSITE/UniProt
| site_id | PS00168 |
| Number of Residues | 15 |
| Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LvHgGAHKtNnaIgQ |
| Chain | Residue | Details |
| B | LEU75-GLN89 | |
| A | LEU75-GLN89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| B | LLP82 | |
| C | LLP82 |
