2GN1
Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 2.2A resolution (Triclinic form with one dimer of TdcB in the asymmetric unit)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0016829 | molecular_function | lyase activity |
| A | 0016841 | molecular_function | ammonia-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0070689 | biological_process | L-threonine catabolic process to propionate |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0016829 | molecular_function | lyase activity |
| B | 0016841 | molecular_function | ammonia-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0070689 | biological_process | L-threonine catabolic process to propionate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 400 |
| Chain | Residue |
| A | TYR220 |
| A | ASP256 |
| A | HOH465 |
| A | HOH466 |
| A | HOH550 |
| B | ARG229 |
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 | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 |
