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 | 0008652 | biological_process | amino acid biosynthetic 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11756443, ECO:0007744|PDB:1KL7 |
| Chain | Residue | Details |
| A | GLY277 | |
| B | THR449 | |
| A | ASN278 | |
| A | PHE279 | |
| A | ASP281 | |
| A | THR449 | |
| B | GLY277 | |
| B | ASN278 | |
| B | PHE279 | |
| B | ASP281 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000305|PubMed:11756443, ECO:0007744|PDB:1KL7 |
| Chain | Residue | Details |
| A | LYS124 | |
| B | LYS124 |
| site_id | SWS_FT_FI3 |
| 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 | GLY132 | 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 | GLY132 | covalently attached, electron pair acceptor, electron pair donor, increase nucleophilicity, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
