5TEJ
Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Vibrio vulnificus with 2,5 Furan 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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 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 |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| D | 0009085 | biological_process | lysine biosynthetic process |
| D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| D | 0019877 | biological_process | diaminopimelate biosynthetic process |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY8 |
| A | SER80 |
| A | GLY98 |
| A | THR99 |
| A | THR100 |
| A | ALA122 |
| A | PRO123 |
| A | ASN124 |
| A | TYR125 |
| A | ARG236 |
| A | GLY11 |
| A | ARG12 |
| A | MET13 |
| A | SER33 |
| A | GLU34 |
| A | ARG35 |
| A | PHE75 |
| A | THR76 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 A 302 |
| Chain | Residue |
| A | GLY192 |
| A | ILE193 |
| C | GLY101 |
| C | ALA162 |
| C | PRO163 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY8 |
| B | GLY11 |
| B | ARG12 |
| B | MET13 |
| B | SER33 |
| B | GLU34 |
| B | ARG35 |
| B | PHE75 |
| B | THR76 |
| B | SER80 |
| B | GLY98 |
| B | THR100 |
| B | ALA122 |
| B | PRO123 |
| B | ASN124 |
| B | TYR125 |
| B | LYS159 |
| B | PHE239 |
| B | 7FN302 |
| B | HOH401 |
| B | HOH419 |
| B | HOH422 |
| B | HOH425 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue 7FN B 302 |
| Chain | Residue |
| B | THR100 |
| B | PRO123 |
| B | HIS156 |
| B | LYS159 |
| B | SER164 |
| B | GLY165 |
| B | THR166 |
| B | NAD301 |
| B | HOH401 |
| B | HOH403 |
| B | HOH425 |
| B | HOH428 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 303 |
| Chain | Residue |
| A | GLN109 |
| A | HOH451 |
| B | ALA21 |
| B | HIS22 |
| B | ASN24 |
| B | ALA27 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PGE B 304 |
| Chain | Residue |
| B | GLY101 |
| B | ALA162 |
| B | ILE168 |
| D | GLU191 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue NAD C 301 |
| Chain | Residue |
| C | GLY8 |
| C | GLY11 |
| C | ARG12 |
| C | MET13 |
| C | SER33 |
| C | GLU34 |
| C | ARG35 |
| C | PHE75 |
| C | THR76 |
| C | SER80 |
| C | GLY98 |
| C | THR100 |
| C | ALA122 |
| C | PRO123 |
| C | ASN124 |
| C | TYR125 |
| C | LYS159 |
| C | 7FN302 |
| C | HOH401 |
| C | HOH402 |
| C | HOH408 |
| C | HOH410 |
| C | HOH416 |
| C | HOH422 |
| C | HOH436 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue 7FN C 302 |
| Chain | Residue |
| C | GLY165 |
| C | THR166 |
| C | NAD301 |
| C | HOH402 |
| C | HOH405 |
| C | HOH410 |
| C | THR100 |
| C | PRO123 |
| C | HIS155 |
| C | HIS156 |
| C | LYS159 |
| C | SER164 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 303 |
| Chain | Residue |
| C | ALA21 |
| C | HIS22 |
| C | ASN24 |
| C | ALA27 |
| D | GLN109 |
| D | HOH470 |
| site_id | AD1 |
| Number of Residues | 25 |
| Details | binding site for residue NAD D 301 |
| Chain | Residue |
| D | GLY8 |
| D | GLY11 |
| D | ARG12 |
| D | MET13 |
| D | SER33 |
| D | GLU34 |
| D | ARG35 |
| D | PHE75 |
| D | THR76 |
| D | SER80 |
| D | GLY98 |
| D | THR100 |
| D | ALA122 |
| D | PRO123 |
| D | ASN124 |
| D | TYR125 |
| D | LYS159 |
| D | PHE239 |
| D | 7FN302 |
| D | HOH402 |
| D | HOH420 |
| D | HOH422 |
| D | HOH440 |
| D | HOH443 |
| D | HOH448 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue 7FN D 302 |
| Chain | Residue |
| D | THR100 |
| D | PRO123 |
| D | HIS156 |
| D | LYS159 |
| D | SER164 |
| D | GLY165 |
| D | THR166 |
| D | NAD301 |
| D | HOH402 |
| D | HOH411 |
| D | HOH414 |
| D | HOH422 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 303 |
| Chain | Residue |
| D | ALA21 |
| D | HIS22 |
| D | ASN24 |
| D | ALA27 |
| D | HOH472 |
| D | HOH474 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 304 |
| Chain | Residue |
| D | GLY179 |
| D | ASN180 |
| D | HOH444 |
| D | HOH449 |
| D | HOH457 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EIvEaHhrhKvDapSGTA |
| Chain | Residue | Details |
| A | GLU150-ALA167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | HIS155 | |
| B | HIS155 | |
| C | HIS155 | |
| D | HIS155 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | LYS159 | |
| B | LYS159 | |
| C | LYS159 | |
| D | LYS159 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | GLY8 | |
| B | ARG35 | |
| B | GLY98 | |
| B | ALA122 | |
| B | HIS156 | |
| B | GLY165 | |
| C | GLY8 | |
| C | GLU34 | |
| C | ARG35 | |
| C | GLY98 | |
| C | ALA122 | |
| A | GLU34 | |
| C | HIS156 | |
| C | GLY165 | |
| D | GLY8 | |
| D | GLU34 | |
| D | ARG35 | |
| D | GLY98 | |
| D | ALA122 | |
| D | HIS156 | |
| D | GLY165 | |
| A | ARG35 | |
| A | GLY98 | |
| A | ALA122 | |
| A | HIS156 | |
| A | GLY165 | |
| B | GLY8 | |
| B | GLU34 |
