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 | 0003824 | molecular_function | catalytic activity |
A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008721 | molecular_function | D-serine 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 | 0003824 | molecular_function | catalytic activity |
B | 0003941 | molecular_function | L-serine ammonia-lyase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0008721 | molecular_function | D-serine 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 | 0003824 | molecular_function | catalytic activity |
C | 0003941 | molecular_function | L-serine ammonia-lyase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0008721 | molecular_function | D-serine 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 | 0003824 | molecular_function | catalytic activity |
D | 0003941 | molecular_function | L-serine ammonia-lyase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0008721 | molecular_function | D-serine 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 |