Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004795 | molecular_function | threonine synthase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | SER247 |
A | GLY248 |
A | ASN249 |
A | PHE250 |
A | GLY251 |
A | ASP252 |
A | KPA500 |
A | HOH538 |
A | HOH672 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE KPA A 500 |
Chain | Residue |
A | LYS107 |
A | THR133 |
A | SER134 |
A | ASP136 |
A | THR137 |
A | PHE186 |
A | ASN212 |
A | SER213 |
A | ARG218 |
A | ASN249 |
A | SO4501 |
A | HOH503 |
A | HOH538 |
A | HOH630 |
Functional Information from PROSITE/UniProt
site_id | PS00165 |
Number of Residues | 15 |
Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. ElfhgpTLAFKDFGG |
Chain | Residue | Details |
A | GLU97-GLY111 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS107 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1pwh |
Chain | Residue | Details |
A | LYS107 | |