3AEY
Apo form of threonine synthase from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008652 | biological_process | amino acid biosynthetic 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 |
| 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 | 0008652 | biological_process | amino acid biosynthetic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | LYS61 |
| A | SER84 |
| A | THR88 |
| A | SER155 |
| A | ARG160 |
| A | ASN188 |
| A | HOH424 |
| A | HOH451 |
| A | HOH661 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG229 |
| A | VAL231 |
| A | GLU232 |
| A | ARG233 |
| A | GLN250 |
| A | HOH404 |
| A | HOH586 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | LYS61 |
| A | SER84 |
| A | GLY86 |
| A | ASN87 |
| A | THR88 |
| A | ALA240 |
| A | HOH431 |
| A | HOH494 |
| A | HOH500 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | PHE60 |
| A | VAL186 |
| A | GLY187 |
| A | ASN188 |
| A | ALA189 |
| A | GLY190 |
| A | ASN191 |
| A | HOH356 |
| A | HOH357 |
| A | HOH360 |
| A | HOH378 |
| A | HOH451 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ILE243 |
| A | GLY244 |
| A | ASN245 |
| A | HOH475 |
| A | HOH524 |
| A | HOH572 |
| A | HOH633 |
| A | HOH676 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | LYS61 |
| B | THR85 |
| B | GLY86 |
| B | ASN87 |
| B | THR88 |
| B | ALA240 |
| B | HOH380 |
| B | HOH508 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | ARG229 |
| B | VAL231 |
| B | GLU232 |
| B | ARG233 |
| B | HOH417 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | PHE60 |
| B | VAL186 |
| B | GLY187 |
| B | ASN188 |
| B | ALA189 |
| B | GLY190 |
| B | ASN191 |
| B | HOH362 |
| B | HOH371 |
| B | HOH384 |
| B | HOH485 |
| B | HOH582 |
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 |
