1UIN
Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| A | 0004794 | molecular_function | threonine deaminase activity |
| A | 0004795 | molecular_function | threonine synthase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0006567 | biological_process | threonine catabolic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| B | 0004794 | molecular_function | threonine deaminase activity |
| B | 0004795 | molecular_function | threonine synthase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006565 | biological_process | L-serine catabolic process |
| B | 0006567 | biological_process | threonine catabolic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
| Chain | Residue |
| B | SER84 |
| B | THR88 |
| B | SER155 |
| B | ARG160 |
| B | ASN188 |
| B | HOH1556 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | ARG233 |
| A | GLN250 |
| A | HOH1114 |
| A | ARG229 |
| A | VAL231 |
| A | GLU232 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | ILE243 |
| A | GLY244 |
| A | ASN245 |
| A | HOH1073 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP A 513 |
| Chain | Residue |
| A | SER59 |
| A | PHE60 |
| A | LYS61 |
| A | ASN87 |
| A | VAL186 |
| A | GLY187 |
| A | ASN188 |
| A | ALA189 |
| A | GLY190 |
| A | ASN191 |
| A | ALA240 |
| A | GLU287 |
| A | THR317 |
| A | GLY318 |
| A | HOH1008 |
| A | HOH1010 |
| A | HOH1044 |
| A | HOH1103 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 1513 |
| Chain | Residue |
| B | PHE60 |
| B | LYS61 |
| B | ASN87 |
| B | VAL186 |
| B | GLY187 |
| B | ASN188 |
| B | ALA189 |
| B | GLY190 |
| B | ASN191 |
| B | ALA240 |
| B | GLU287 |
| B | THR317 |
| B | GLY318 |
| B | HOH1515 |
| B | HOH1516 |
| B | HOH1529 |
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 | GLU52-MET65 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| A | LYS61 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| B | LYS61 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| A | LYS61 | |
| A | THR317 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pwh |
| Chain | Residue | Details |
| B | LYS61 | |
| B | THR317 |
