2EJW
Homoserine Dehydrogenase from Thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004412 | molecular_function | homoserine dehydrogenase activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050661 | molecular_function | NADP binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004412 | molecular_function | homoserine dehydrogenase activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0009088 | biological_process | threonine biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050661 | molecular_function | NADP binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004412 | molecular_function | homoserine dehydrogenase activity |
E | 0006520 | biological_process | amino acid metabolic process |
E | 0009086 | biological_process | methionine biosynthetic process |
E | 0009088 | biological_process | threonine biosynthetic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0050661 | molecular_function | NADP binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0004412 | molecular_function | homoserine dehydrogenase activity |
F | 0006520 | biological_process | amino acid metabolic process |
F | 0009086 | biological_process | methionine biosynthetic process |
F | 0009088 | biological_process | threonine biosynthetic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 2003 |
Chain | Residue |
A | GLU121 |
A | VAL124 |
A | ALA126 |
A | THR128 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 2002 |
Chain | Residue |
A | HOH2807 |
A | ASP68 |
A | HOH2622 |
A | HOH2652 |
A | HOH2663 |
A | HOH2779 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 A 2602 |
Chain | Residue |
A | ASN150 |
A | GLY151 |
A | THR152 |
A | ASP191 |
A | LYS195 |
A | GLY288 |
A | HOH2772 |
A | HOH2820 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 2001 |
Chain | Residue |
A | MET1 |
B | GLU114 |
B | HOH2504 |
B | HOH2509 |
B | HOH2517 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 2004 |
Chain | Residue |
B | GLU121 |
B | VAL124 |
B | ALA126 |
B | THR128 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 2006 |
Chain | Residue |
E | GLU121 |
E | VAL124 |
E | MET125 |
E | ALA126 |
E | THR128 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 2007 |
Chain | Residue |
E | GLU24 |
E | HOH2639 |
E | HOH2652 |
E | HOH2700 |
F | HOH2729 |
F | HOH2776 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NO3 E 2601 |
Chain | Residue |
E | GLY151 |
E | THR152 |
E | TYR178 |
E | LYS195 |
E | GLY288 |
E | ALA289 |
E | HOH2702 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 2005 |
Chain | Residue |
F | GLU121 |
F | VAL124 |
F | MET125 |
F | ALA126 |
F | THR128 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 F 2603 |
Chain | Residue |
F | ASN150 |
F | GLY151 |
F | THR152 |
F | LYS195 |
F | GLY288 |
F | ALA289 |
F | HOH2654 |
F | HOH2832 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 2501 |
Chain | Residue |
B | GLY151 |
B | TYR178 |
B | ASN270 |
B | PRO287 |
B | GLY288 |
B | HOH2543 |
B | HOH2646 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL E 2502 |
Chain | Residue |
E | GLU135 |
E | ARG304 |
E | HOH2602 |
E | HOH2605 |
E | HOH2616 |
E | HOH2756 |
F | ARG304 |
F | SER307 |
Functional Information from PROSITE/UniProt
site_id | PS01042 |
Number of Residues | 23 |
Details | HOMOSER_DHGENASE Homoserine dehydrogenase signature. AqrlGYAea.DPtlDVeGiDaahK |
Chain | Residue | Details |
A | ALA173-LYS195 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ebf |
Chain | Residue | Details |
A | LYS195 | |
A | ASP191 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ebf |
Chain | Residue | Details |
B | LYS195 | |
B | ASP191 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ebf |
Chain | Residue | Details |
E | LYS195 | |
E | ASP191 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ebf |
Chain | Residue | Details |
F | LYS195 | |
F | ASP191 |