2D1F
Structure of Mycobacterium tuberculosis threonine synthase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004795 | molecular_function | threonine synthase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
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 | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP A 500 |
Chain | Residue |
A | SER67 |
A | ASN200 |
A | GLU296 |
A | THR326 |
A | HOH503 |
A | HOH507 |
A | HOH524 |
A | PHE68 |
A | LYS69 |
A | ASN95 |
A | VAL195 |
A | GLY196 |
A | ASN197 |
A | ALA198 |
A | GLY199 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP B 500 |
Chain | Residue |
B | SER67 |
B | PHE68 |
B | LYS69 |
B | ASN95 |
B | VAL195 |
B | GLY196 |
B | ASN197 |
B | ALA198 |
B | GLY199 |
B | ASN200 |
B | GLU296 |
B | ALA298 |
B | THR326 |
B | GLY327 |
B | HOH502 |
B | HOH503 |
B | HOH507 |
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 | GLU60-MET73 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18621388 |
Chain | Residue | Details |
A | ASN95 | |
B | GLY196 | |
B | THR326 | |
A | GLY196 | |
A | THR326 | |
B | ASN95 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18621388 |
Chain | Residue | Details |
A | LYS69 | |
B | LYS69 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036 |
Chain | Residue | Details |
A | LYS151 | |
B | LYS151 |