4F4F
X-Ray crystal structure of PLP bound Threonine synthase from Brucella melitensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004795 | molecular_function | threonine synthase activity |
| 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 | 0003824 | molecular_function | catalytic activity |
| B | 0004795 | molecular_function | threonine synthase activity |
| 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 | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | PHE111 |
| A | SER307 |
| A | HIS386 |
| A | THR409 |
| A | ALA410 |
| A | HOH765 |
| A | HOH795 |
| A | HOH812 |
| A | HOH924 |
| A | LYS112 |
| A | PRO253 |
| A | THR254 |
| A | GLY255 |
| A | ASN256 |
| A | PHE257 |
| A | GLY258 |
| A | ASP259 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| B | PHE111 |
| B | LYS112 |
| B | PRO253 |
| B | THR254 |
| B | GLY255 |
| B | ASN256 |
| B | PHE257 |
| B | GLY258 |
| B | ASP259 |
| B | SER307 |
| B | HIS386 |
| B | THR409 |
| B | ALA410 |
| B | HOH669 |
| B | HOH718 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 15 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. ElfhgpTLAFKDVAM |
| Chain | Residue | Details |
| A | GLU102-MET116 |
