5TEM
Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Vibrio vulnificus with 2,6 Pyridine Dicarboxylic and NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| C | 0009085 | biological_process | lysine biosynthetic process |
| C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| C | 0019877 | biological_process | diaminopimelate biosynthetic process |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue NAD C 1001 |
| Chain | Residue |
| C | GLY8 |
| C | SER80 |
| C | GLY98 |
| C | THR100 |
| C | ALA122 |
| C | PRO123 |
| C | ASN124 |
| C | TYR125 |
| C | LYS159 |
| C | PDC1002 |
| C | HOH1112 |
| C | GLY11 |
| C | HOH1126 |
| C | HOH1128 |
| C | HOH1145 |
| C | HOH1157 |
| C | HOH1160 |
| C | HOH1181 |
| C | ARG12 |
| C | MET13 |
| C | SER33 |
| C | GLU34 |
| C | ARG35 |
| C | PHE75 |
| C | THR76 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue PDC C 1002 |
| Chain | Residue |
| C | THR100 |
| C | PRO123 |
| C | HIS156 |
| C | LYS159 |
| C | SER164 |
| C | GLY165 |
| C | THR166 |
| C | NAD1001 |
| C | HOH1112 |
| C | HOH1129 |
| C | HOH1145 |
| C | HOH1156 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 1003 |
| Chain | Residue |
| A | GLN89 |
| C | LYS19 |
| C | HIS23 |
| C | MET237 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 1001 |
| Chain | Residue |
| A | GLY8 |
| A | GLY11 |
| A | ARG12 |
| A | MET13 |
| A | SER33 |
| A | GLU34 |
| A | ARG35 |
| A | PHE75 |
| A | THR76 |
| A | SER80 |
| A | GLY98 |
| A | THR100 |
| A | ALA122 |
| A | PRO123 |
| A | ASN124 |
| A | TYR125 |
| A | LYS159 |
| A | PHE239 |
| A | PDC1002 |
| A | HOH1116 |
| A | HOH1122 |
| A | HOH1130 |
| A | HOH1148 |
| A | HOH1154 |
| A | HOH1165 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue PDC A 1002 |
| Chain | Residue |
| A | THR100 |
| A | PRO123 |
| A | HIS156 |
| A | LYS159 |
| A | SER164 |
| A | GLY165 |
| A | THR166 |
| A | NAD1001 |
| A | HOH1123 |
| A | HOH1130 |
| A | HOH1165 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1003 |
| Chain | Residue |
| A | GLU37 |
| A | SER38 |
| A | SER39 |
| A | HOH1182 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1004 |
| Chain | Residue |
| A | ARG157 |
| A | HIS158 |
| A | ILE223 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1005 |
| Chain | Residue |
| A | THR103 |
| A | GLU104 |
| A | HOH1187 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EIvEaHhrhKvDapSGTA |
| Chain | Residue | Details |
| C | GLU150-ALA167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






