5TEK
Apo Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Mycobacterium tuberculosis
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 |
| 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 | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | GLY143 |
| A | THR144 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | VAL21 |
| A | ALA22 |
| A | ALA24 |
| A | LEU27 |
| A | HOH444 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | GLY143 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | HIS134 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 B 303 |
| Chain | Residue |
| A | GLU196 |
| B | GLU196 |
| B | ARG209 |
| B | ASP211 |
| B | PG4304 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 B 304 |
| Chain | Residue |
| A | LEU132 |
| A | LEU191 |
| A | GLU196 |
| A | ARG209 |
| A | ASP211 |
| B | GLU196 |
| B | PG4303 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 305 |
| Chain | Residue |
| B | VAL21 |
| B | ALA22 |
| B | ALA24 |
| B | LEU27 |
| B | HOH486 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EViElHhphKaDapSGTA |
| Chain | Residue | Details |
| A | GLU128-ALA145 |
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 | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
