1ARZ
ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE
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 | 0042802 | molecular_function | identical protein binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 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 | 0042802 | molecular_function | identical protein binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0042802 | molecular_function | identical protein binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 301 |
| Chain | Residue |
| A | HIS160 |
| A | LYS163 |
| A | VAL217 |
| A | ARG240 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 301 |
| Chain | Residue |
| B | ALA25 |
| B | LEU26 |
| B | LEU28 |
| B | VAL31 |
| B | HOH411 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAI B 302 |
| Chain | Residue |
| B | GLY12 |
| B | GLY14 |
| B | GLY15 |
| B | ARG16 |
| B | MET17 |
| B | GLU38 |
| B | PHE79 |
| B | THR80 |
| B | ARG81 |
| B | GLY84 |
| B | HIS88 |
| B | GLY102 |
| B | THR104 |
| B | ALA127 |
| B | ASN128 |
| B | PHE129 |
| B | LYS163 |
| B | PHE243 |
| B | PDC303 |
| B | HOH415 |
| B | HOH425 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PDC B 303 |
| Chain | Residue |
| B | THR104 |
| B | ALA127 |
| B | HIS160 |
| B | LYS163 |
| B | SER168 |
| B | GLY169 |
| B | THR170 |
| B | NAI302 |
| B | HOH425 |
| B | HOH435 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI C 301 |
| Chain | Residue |
| B | HOH404 |
| C | GLY12 |
| C | GLY15 |
| C | ARG16 |
| C | MET17 |
| C | GLU38 |
| C | PHE79 |
| C | THR80 |
| C | ARG81 |
| C | GLY84 |
| C | GLY102 |
| C | THR103 |
| C | THR104 |
| C | ALA127 |
| C | PHE129 |
| C | LYS163 |
| C | PHE243 |
| C | PDC302 |
| C | HOH406 |
| C | HOH410 |
| C | HOH422 |
| C | HOH423 |
| C | HOH439 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PDC C 302 |
| Chain | Residue |
| C | THR104 |
| C | ALA127 |
| C | HIS160 |
| C | LYS163 |
| C | SER168 |
| C | GLY169 |
| C | THR170 |
| C | NAI301 |
| C | HOH439 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 301 |
| Chain | Residue |
| D | ASP3 |
| D | ALA25 |
| D | LEU26 |
| D | LEU28 |
| D | VAL31 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI D 302 |
| Chain | Residue |
| D | HOH440 |
| D | GLY12 |
| D | GLY14 |
| D | GLY15 |
| D | ARG16 |
| D | MET17 |
| D | GLU38 |
| D | ARG39 |
| D | PHE79 |
| D | THR80 |
| D | ARG81 |
| D | GLY84 |
| D | GLY102 |
| D | THR103 |
| D | THR104 |
| D | ALA127 |
| D | ASN128 |
| D | PHE129 |
| D | LYS163 |
| D | PHE243 |
| D | PDC303 |
| D | HOH426 |
| D | HOH433 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PDC D 303 |
| Chain | Residue |
| D | THR104 |
| D | ALA127 |
| D | HIS160 |
| D | LYS163 |
| D | SER168 |
| D | GLY169 |
| D | THR170 |
| D | NAI302 |
| D | HOH413 |
| D | HOH415 |
| D | HOH433 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EIiEaHhrhKvDapSGTA |
| Chain | Residue | Details |
| A | GLU154-ALA171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor |
| Chain | Residue | Details |
| A | HIS159 | |
| B | HIS159 | |
| C | HIS159 | |
| D | HIS159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | LYS163 | |
| B | LYS163 | |
| C | LYS163 | |
| D | LYS163 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7893645, ECO:0007744|PDB:1DIH |
| Chain | Residue | Details |
| A | GLY12 | |
| B | GLY102 | |
| B | PHE129 | |
| B | ARG240 | |
| C | GLY12 | |
| C | ARG16 | |
| C | ARG39 | |
| C | GLY102 | |
| C | PHE129 | |
| C | ARG240 | |
| D | GLY12 | |
| A | ARG16 | |
| D | ARG16 | |
| D | ARG39 | |
| D | GLY102 | |
| D | PHE129 | |
| D | ARG240 | |
| A | ARG39 | |
| A | GLY102 | |
| A | PHE129 | |
| A | ARG240 | |
| B | GLY12 | |
| B | ARG16 | |
| B | ARG39 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8873595, ECO:0000269|PubMed:9398235, ECO:0007744|PDB:1ARZ, ECO:0007744|PDB:1DRU |
| Chain | Residue | Details |
| A | GLY15 | |
| C | GLU38 | |
| C | THR80 | |
| C | ALA126 | |
| D | GLY15 | |
| D | GLU38 | |
| D | THR80 | |
| D | ALA126 | |
| A | GLU38 | |
| A | THR80 | |
| A | ALA126 | |
| B | GLY15 | |
| B | GLU38 | |
| B | THR80 | |
| B | ALA126 | |
| C | GLY15 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS160 | |
| A | GLY169 | |
| B | HIS160 | |
| B | GLY169 | |
| C | HIS160 | |
| C | GLY169 | |
| D | HIS160 | |
| D | GLY169 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9398235, ECO:0007744|PDB:1ARZ |
| Chain | Residue | Details |
| A | LYS163 | |
| A | PHE243 | |
| B | LYS163 | |
| B | PHE243 | |
| C | LYS163 | |
| C | PHE243 | |
| D | LYS163 | |
| D | PHE243 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 9398235 |
| Chain | Residue | Details |
| A | LYS163 | |
| A | HIS159 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 402 |
| Chain | Residue | Details |
| A | HIS159 | activator, proton shuttle (general acid/base) |
| A | LYS163 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 402 |
| Chain | Residue | Details |
| B | HIS159 | activator, proton shuttle (general acid/base) |
| B | LYS163 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 402 |
| Chain | Residue | Details |
| C | HIS159 | activator, proton shuttle (general acid/base) |
| C | LYS163 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 402 |
| Chain | Residue | Details |
| D | HIS159 | activator, proton shuttle (general acid/base) |
| D | LYS163 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
