4XB1
Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH
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 | 0009090 | biological_process | homoserine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070403 | molecular_function | NAD+ 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 | 0009090 | biological_process | homoserine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue NDP A 1001 |
| Chain | Residue |
| A | PHE8 |
| A | SER92 |
| A | SER93 |
| A | SER114 |
| A | ASN115 |
| A | LYS116 |
| A | SER141 |
| A | GLY295 |
| A | GLY296 |
| A | THR300 |
| A | MPD1003 |
| A | PHE10 |
| A | HOH1143 |
| A | HOH1161 |
| A | HOH1170 |
| A | HOH1201 |
| A | HOH1205 |
| A | HOH1211 |
| A | HOH1213 |
| A | HOH1219 |
| A | GLY11 |
| A | THR12 |
| A | VAL13 |
| A | ASP39 |
| A | ARG40 |
| A | LYS57 |
| A | VAL91 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 1002 |
| Chain | Residue |
| A | GLU140 |
| A | VAL143 |
| A | MET144 |
| A | ALA145 |
| A | THR147 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 1003 |
| Chain | Residue |
| A | LYS116 |
| A | LYS215 |
| A | GLY294 |
| A | NDP1001 |
| A | HOH1144 |
| A | HOH1188 |
| A | HOH1201 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MPD A 1004 |
| Chain | Residue |
| A | LYS131 |
| A | GLY225 |
| A | LEU318 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue NDP B 1001 |
| Chain | Residue |
| B | PHE8 |
| B | PHE10 |
| B | GLY11 |
| B | THR12 |
| B | VAL13 |
| B | ASP39 |
| B | ARG40 |
| B | LYS57 |
| B | VAL91 |
| B | SER92 |
| B | SER93 |
| B | SER114 |
| B | ASN115 |
| B | LYS116 |
| B | SER141 |
| B | GLY295 |
| B | GLY296 |
| B | THR300 |
| B | MPD1003 |
| B | HOH1125 |
| B | HOH1163 |
| B | HOH1174 |
| B | HOH1188 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 1002 |
| Chain | Residue |
| B | GLU140 |
| B | VAL143 |
| B | MET144 |
| B | ALA145 |
| B | THR147 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MPD B 1003 |
| Chain | Residue |
| B | LYS116 |
| B | LYS215 |
| B | GLY294 |
| B | NDP1001 |
| B | HOH1163 |
| B | HOH1178 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 1004 |
| Chain | Residue |
| A | ASN73 |
| A | GLU78 |
| B | ASN267 |
| B | HOH1103 |
| B | HOH1109 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue MPD B 1005 |
| Chain | Residue |
| B | MET127 |
| B | GLY225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PIRSR:PIRSR036497-1 |
| Chain | Residue | Details |
| A | LYS215 | |
| B | LYS215 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26154028, ECO:0007744|PDB:4XB1, ECO:0007744|PDB:4XB2 |
| Chain | Residue | Details |
| A | PHE10 | |
| A | VAL143 | |
| A | ALA145 | |
| A | THR147 | |
| A | GLY296 | |
| B | PHE10 | |
| B | THR12 | |
| B | VAL13 | |
| B | ARG40 | |
| B | SER92 | |
| B | SER93 | |
| A | THR12 | |
| B | SER114 | |
| B | LYS116 | |
| B | GLU140 | |
| B | VAL143 | |
| B | ALA145 | |
| B | THR147 | |
| B | GLY296 | |
| A | VAL13 | |
| A | ARG40 | |
| A | SER92 | |
| A | SER93 | |
| A | SER114 | |
| A | LYS116 | |
| A | GLU140 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26154028, ECO:0007744|PDB:4XB1 |
| Chain | Residue | Details |
| A | LYS57 | |
| B | LYS57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:F9VNG5 |
| Chain | Residue | Details |
| A | GLY197 | |
| A | GLU200 | |
| B | GLY197 | |
| B | GLU200 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31116 |
| Chain | Residue | Details |
| A | ASP211 | |
| B | ASP211 |
