2GN0
Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 1.7 A resolution (Triclinic form with one complete subunit built in alternate conformation)
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 | 0006520 | biological_process | amino acid metabolic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0006567 | biological_process | L-threonine catabolic process |
| A | 0016841 | molecular_function | ammonia-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 | 0006520 | biological_process | amino acid metabolic process |
| B | 0006565 | biological_process | L-serine catabolic process |
| B | 0006567 | biological_process | L-threonine catabolic process |
| B | 0016841 | molecular_function | ammonia-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| C | 0004794 | molecular_function | threonine deaminase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006565 | biological_process | L-serine catabolic process |
| C | 0006567 | biological_process | L-threonine catabolic process |
| C | 0016841 | molecular_function | ammonia-lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| D | 0004794 | molecular_function | threonine deaminase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006565 | biological_process | L-serine catabolic process |
| D | 0006567 | biological_process | L-threonine catabolic process |
| D | 0016841 | molecular_function | ammonia-lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 800 |
| Chain | Residue |
| A | TYR220 |
| A | ASP256 |
| A | HOH801 |
| A | HOH802 |
| A | HOH803 |
| D | ARG229 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 801 |
| Chain | Residue |
| C | ASP256 |
| C | HOH815 |
| C | HOH983 |
| B | ARG229 |
| B | HOH338 |
| C | TYR220 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Enmqr.TGSFKIRGA |
| Chain | Residue | Details |
| A | GLU49-ALA62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| A | SER311 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| B | SER311 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| C | SER311 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| D | SER311 |
