1KL7
Crystal Structure of Threonine Synthase from Yeast
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004795 | molecular_function | threonine synthase activity |
A | 0005634 | cellular_component | nucleus |
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 | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0004795 | molecular_function | threonine synthase activity |
B | 0005634 | cellular_component | nucleus |
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 | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLP A 1400 |
Chain | Residue |
A | PHE123 |
A | ALA330 |
A | HIS422 |
A | THR449 |
A | ALA450 |
A | HOH1401 |
A | HOH1454 |
A | HOH1548 |
A | LYS124 |
A | ASP163 |
A | SER276 |
A | GLY277 |
A | ASN278 |
A | PHE279 |
A | GLY280 |
A | ASP281 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLP B 1400 |
Chain | Residue |
B | PHE123 |
B | LYS124 |
B | ASP163 |
B | SER276 |
B | GLY277 |
B | ASN278 |
B | PHE279 |
B | GLY280 |
B | ASP281 |
B | ALA330 |
B | HIS422 |
B | THR449 |
B | ALA450 |
B | HOH1405 |
B | HOH1442 |
B | HOH1572 |
Functional Information from PROSITE/UniProt
site_id | PS00165 |
Number of Residues | 15 |
Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. ElfhgpTYAFKDVAL |
Chain | Residue | Details |
A | GLU114-LEU128 |
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 |
A | LYS124 | |
B | LYS124 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER467 | |
B | SER467 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
A | LYS124 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 730 |
Chain | Residue | Details |
A | LYS124 | covalently attached, electron pair acceptor, electron pair donor, increase nucleophilicity, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 730 |
Chain | Residue | Details |
B | LYS124 | covalently attached, electron pair acceptor, electron pair donor, increase nucleophilicity, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |