1V7C
Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue
Replaces: 1UIQFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004795 | molecular_function | threonine synthase activity |
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 | 0019344 | biological_process | cysteine biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 1901605 | biological_process | alpha-amino acid metabolic process |
B | 0004795 | molecular_function | threonine synthase activity |
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 | 0019344 | biological_process | cysteine biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 1901605 | biological_process | alpha-amino acid metabolic process |
C | 0004795 | molecular_function | threonine synthase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0009088 | biological_process | threonine biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0019344 | biological_process | cysteine biosynthetic process |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 1901605 | biological_process | alpha-amino acid metabolic process |
D | 0004795 | molecular_function | threonine synthase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0009088 | biological_process | threonine biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0019344 | biological_process | cysteine biosynthetic process |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEY A 1400 |
Chain | Residue |
A | PHE60 |
A | ARG160 |
A | VAL186 |
A | GLY187 |
A | ASN188 |
A | ALA189 |
A | GLY190 |
A | ASN191 |
A | ALA240 |
A | ILE241 |
A | GLU287 |
A | LYS61 |
A | THR317 |
A | HOH1402 |
A | HOH1406 |
A | HOH1427 |
A | HOH1441 |
A | HOH1465 |
A | SER84 |
A | THR85 |
A | ASN87 |
A | THR88 |
A | PHE134 |
A | ASN154 |
A | SER155 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEY B 2400 |
Chain | Residue |
B | PHE60 |
B | LYS61 |
B | SER84 |
B | THR85 |
B | ASN87 |
B | THR88 |
B | PHE134 |
B | ASN154 |
B | SER155 |
B | ARG160 |
B | VAL186 |
B | GLY187 |
B | ASN188 |
B | ALA189 |
B | GLY190 |
B | ASN191 |
B | ALA240 |
B | ILE241 |
B | GLU287 |
B | THR317 |
B | HOH2402 |
B | HOH2403 |
B | HOH2413 |
B | HOH2422 |
B | HOH2514 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEY C 3400 |
Chain | Residue |
C | PHE60 |
C | LYS61 |
C | SER84 |
C | THR85 |
C | ASN87 |
C | THR88 |
C | PHE134 |
C | ASN154 |
C | SER155 |
C | ARG160 |
C | PRO185 |
C | VAL186 |
C | GLY187 |
C | ASN188 |
C | ALA189 |
C | GLY190 |
C | ASN191 |
C | ALA240 |
C | ILE241 |
C | GLU287 |
C | THR317 |
C | HOH3408 |
C | HOH3416 |
C | HOH3449 |
C | HOH3462 |
C | HOH3512 |
site_id | AC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEY D 4400 |
Chain | Residue |
D | HOH4448 |
D | HOH4581 |
D | PHE60 |
D | LYS61 |
D | SER84 |
D | THR85 |
D | ASN87 |
D | THR88 |
D | PHE134 |
D | ASN154 |
D | SER155 |
D | ARG160 |
D | VAL186 |
D | GLY187 |
D | ASN188 |
D | ALA189 |
D | GLY190 |
D | ASN191 |
D | ALA240 |
D | ILE241 |
D | GLU287 |
D | THR317 |
D | HOH4401 |
D | HOH4414 |
D | HOH4442 |
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 |