1VE5
Crystal Structure of T.th. HB8 Threonine deaminase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016841 | molecular_function | ammonia-lyase activity |
| A | 0018114 | molecular_function | threonine racemase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030378 | molecular_function | serine racemase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070179 | biological_process | D-serine biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016841 | molecular_function | ammonia-lyase activity |
| B | 0018114 | molecular_function | threonine racemase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030378 | molecular_function | serine racemase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070179 | biological_process | D-serine biosynthetic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016841 | molecular_function | ammonia-lyase activity |
| C | 0018114 | molecular_function | threonine racemase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0030378 | molecular_function | serine racemase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070179 | biological_process | D-serine biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016841 | molecular_function | ammonia-lyase activity |
| D | 0018114 | molecular_function | threonine racemase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0030378 | molecular_function | serine racemase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070179 | biological_process | D-serine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2001 |
| Chain | Residue |
| A | GLU203 |
| A | ALA207 |
| A | ASP209 |
| A | HOH1067 |
| A | HOH1223 |
| A | HOH1231 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA D 2002 |
| Chain | Residue |
| D | GLU203 |
| D | ALA207 |
| D | ASP209 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 2003 |
| Chain | Residue |
| B | GLU203 |
| B | ALA207 |
| B | ASP209 |
| B | HOH1012 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 2004 |
| Chain | Residue |
| C | GLU203 |
| C | ALA207 |
| C | ASP209 |
| C | HOH1063 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | PHE50 |
| A | LYS51 |
| A | ASN75 |
| A | PRO176 |
| A | GLY178 |
| A | GLY179 |
| A | GLY180 |
| A | GLY181 |
| A | LEU182 |
| A | GLU277 |
| A | THR279 |
| A | SER303 |
| A | GLY304 |
| A | HOH1019 |
| A | HOH1109 |
| A | HOH1175 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 913 |
| Chain | Residue |
| B | PHE50 |
| B | LYS51 |
| B | ASN75 |
| B | PRO176 |
| B | VAL177 |
| B | GLY178 |
| B | GLY179 |
| B | GLY180 |
| B | GLY181 |
| B | LEU182 |
| B | GLU277 |
| B | THR279 |
| B | SER303 |
| B | HOH1001 |
| B | HOH1129 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 1413 |
| Chain | Residue |
| C | PHE50 |
| C | LYS51 |
| C | ASN75 |
| C | PRO176 |
| C | GLY178 |
| C | GLY179 |
| C | GLY180 |
| C | GLY181 |
| C | LEU182 |
| C | GLU277 |
| C | THR279 |
| C | SER303 |
| C | HOH1039 |
| C | HOH1043 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D 1913 |
| Chain | Residue |
| D | PHE50 |
| D | LYS51 |
| D | ASN75 |
| D | PRO176 |
| D | GLY178 |
| D | GLY179 |
| D | GLY180 |
| D | GLY181 |
| D | LEU182 |
| D | VAL233 |
| D | GLU277 |
| D | THR279 |
| D | SER303 |
| D | GLY304 |
| D | HOH1008 |
| D | HOH1011 |
| D | HOH1234 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Ehlqk.TGSFKARGA |
| Chain | Residue | Details |
| A | GLU42-ALA55 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS51 | |
| A | THR279 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS51 | |
| B | SER303 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| C | LYS51 | |
| C | SER303 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| D | LYS51 | |
| D | SER303 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS51 | |
| B | THR279 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| C | LYS51 | |
| C | THR279 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| D | LYS51 | |
| D | THR279 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS51 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS51 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| C | LYS51 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| D | LYS51 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS51 | |
| A | SER303 |
