2ZSJ
Crystal structure of threonine synthase from Aquifex aeolicus VF5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004795 | molecular_function | threonine synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004795 | molecular_function | threonine synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004795 | molecular_function | threonine synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0009088 | biological_process | threonine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019344 | biological_process | cysteine biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 1901605 | biological_process | alpha-amino acid metabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004795 | molecular_function | threonine synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0009088 | biological_process | threonine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019344 | biological_process | cysteine biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A1101 |
| Chain | Residue |
| A | SER61 |
| A | ASN193 |
| A | ALA242 |
| A | GLU289 |
| A | THR319 |
| A | GLY320 |
| A | HOH1119 |
| A | HOH1157 |
| A | HOH1198 |
| A | PHE62 |
| A | LYS63 |
| A | ASN89 |
| A | VAL188 |
| A | GLY189 |
| A | ASN190 |
| A | ALA191 |
| A | GLY192 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B1102 |
| Chain | Residue |
| B | PHE62 |
| B | LYS63 |
| B | ASN89 |
| B | VAL188 |
| B | GLY189 |
| B | ASN190 |
| B | ALA191 |
| B | GLY192 |
| B | ASN193 |
| B | ALA242 |
| B | GLU289 |
| B | THR319 |
| B | GLY320 |
| B | HOH1129 |
| B | HOH1170 |
| B | HOH1172 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP C1103 |
| Chain | Residue |
| C | SER61 |
| C | PHE62 |
| C | LYS63 |
| C | ASN89 |
| C | VAL188 |
| C | GLY189 |
| C | ASN190 |
| C | ALA191 |
| C | GLY192 |
| C | ASN193 |
| C | ALA242 |
| C | GLU289 |
| C | THR319 |
| C | GLY320 |
| C | HOH1111 |
| C | HOH1148 |
| C | HOH1176 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D1104 |
| Chain | Residue |
| D | SER61 |
| D | PHE62 |
| D | LYS63 |
| D | ASN89 |
| D | VAL188 |
| D | GLY189 |
| D | ASN190 |
| D | ALA191 |
| D | GLY192 |
| D | ASN193 |
| D | ALA242 |
| D | GLU289 |
| D | THR319 |
| D | GLY320 |
| D | HOH1125 |
| D | HOH1167 |
| D | HOH1177 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Eglnp.TGSFKDRGM |
| Chain | Residue | Details |
| A | GLU54-MET67 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| A | LYS63 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| B | LYS63 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| C | LYS63 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| D | LYS63 |
