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 | 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 | 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 | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
C | HIS155 | |
A | HIS155 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
C | LYS159 | |
A | LYS159 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
C | ARG35 | |
C | GLY98 | |
C | ALA122 | |
C | HIS156 | |
C | GLY165 | |
A | GLY8 | |
A | GLU34 | |
A | ARG35 | |
A | GLY98 | |
A | ALA122 | |
A | HIS156 | |
A | GLY165 | |
C | GLY8 | |
C | GLU34 |